Post-Transcriptional Regulation of the Trypanosome Heat Shock Response by a Zinc Finger Protein
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{"title"=>"Post-Transcriptional Regulation of the Trypanosome Heat Shock Response by a Zinc Finger Protein", "type"=>"journal", "authors"=>[{"first_name"=>"Dorothea", "last_name"=>"Droll", "scopus_author_id"=>"36522651200"}, {"first_name"=>"Igor", "last_name"=>"Minia", "scopus_author_id"=>"55319898100"}, {"first_name"=>"Abeer", "last_name"=>"Fadda", "scopus_author_id"=>"14054035100"}, {"first_name"=>"Aditi", "last_name"=>"Singh", "scopus_author_id"=>"57190229725"}, {"first_name"=>"Mhairi", "last_name"=>"Stewart", "scopus_author_id"=>"55438135500"}, {"first_name"=>"Rafael", "last_name"=>"Queiroz", "scopus_author_id"=>"25629889600"}, {"first_name"=>"Christine", "last_name"=>"Clayton", "scopus_author_id"=>"7201900679"}], "year"=>2013, "source"=>"PLoS Pathogens", "identifiers"=>{"scopus"=>"2-s2.0-84876860902", "sgr"=>"84876860902", "issn"=>"15537366", "arxiv"=>"e1003286", "doi"=>"10.1371/journal.ppat.1003286", "pmid"=>"23592996", "isbn"=>"1553-7374 (Electronic)\\r1553-7366 (Linking)", "pui"=>"368819601"}, "id"=>"b770c482-e32b-307d-8bfb-e7012e1706b9", "abstract"=>"In most organisms, the heat-shock response involves increased heat-shock gene transcription. In Kinetoplastid protists, however, virtually all control of gene expression is post-transcriptional. Correspondingly, Trypanosoma brucei heat-shock protein 70 (HSP70) synthesis after heat shock depends on regulation of HSP70 mRNA turnover. We here show that the T. brucei CCCH zinc finger protein ZC3H11 is a post-transcriptional regulator of trypanosome chaperone mRNAs. ZC3H11 is essential in bloodstream-form trypanosomes and for recovery of insect-form trypanosomes from heat shock. ZC3H11 binds to mRNAs encoding heat-shock protein homologues, with clear specificity for the subset of trypanosome chaperones that is required for protein refolding. In procyclic forms, ZC3H11 was required for stabilisation of target chaperone-encoding mRNAs after heat shock, and the HSP70 mRNA was also decreased upon ZC3H11 depletion in bloodstream forms. Many mRNAs bound to ZC3H11 have a consensus AUU repeat motif in the 3'-untranslated region. ZC3H11 bound preferentially to AUU repeats in vitro, and ZC3H11 regulation of HSP70 mRNA in bloodstream forms depended on its AUU repeat region. Tethering of ZC3H11 to a reporter mRNA increased reporter expression, showing that it is capable of actively stabilizing an mRNA. These results show that expression of trypanosome heat-shock genes is controlled by a specific RNA-protein interaction. They also show that heat-shock-induced chaperone expression in procyclic trypanosome enhances parasite survival at elevated temperatures.", "link"=>"http://www.mendeley.com/research/posttranscriptional-regulation-trypanosome-heat-shock-response-zinc-finger-protein-1", "reader_count"=>41, "reader_count_by_academic_status"=>{"Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>3, "Student > Master"=>10, "Other"=>1, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_user_role"=>{"Professor > Associate Professor"=>1, "Researcher"=>6, "Student > Doctoral Student"=>2, "Student > Ph. D. Student"=>13, "Student > Postgraduate"=>3, "Student > Master"=>10, "Other"=>1, "Student > Bachelor"=>2, "Lecturer"=>1, "Professor"=>2}, "reader_count_by_subject_area"=>{"Biochemistry, Genetics and Molecular Biology"=>8, "Agricultural and Biological Sciences"=>32, "Chemistry"=>1}, "reader_count_by_subdiscipline"=>{"Chemistry"=>{"Chemistry"=>1}, "Agricultural and Biological Sciences"=>{"Agricultural and Biological Sciences"=>32}, "Biochemistry, Genetics and Molecular Biology"=>{"Biochemistry, Genetics and Molecular Biology"=>8}}, "reader_count_by_country"=>{"Czech Republic"=>1, "United States"=>2, "Brazil"=>1, "United Kingdom"=>1}, "group_count"=>2}

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Figshare

  • {"files"=>["https://ndownloader.figshare.com/files/1014515"], "description"=>"<p><b>A.</b> Alignment of ZC3H11 with members of the Tis11 family of several species. The conserved amino acid signature (marked in red) precedes the zinc finger domain (cysteines and histidine shaded in blue). Conserved residues are shaded in yellow and chemically similar ones in orange. Amino acids at the positions marked on the top with # and * are involved in RNA binding by hydrogen bonds or base stacking respectively <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286-Hudson1\" target=\"_blank\">[31]</a>. <b>B.</b> Expression of <i>in situ</i> tagged V5-ZC3H11 in procyclic cells under different conditions. The incubation temperature is shown above along with the duration of the incubation. Treatment with puromycin was for one hour (lanes 11–13). 10<sup>7</sup>cells were loaded per lane; detection was with anti-V5 antibody and with anti-aldolase as loading control. <b>C.</b> Expression of <i>in situ</i> tagged V5-ZC3H11 in bloodstream-form trypanosomes under different conditions. Details are as for (B) <b>D.</b> Effect of proteasome inhibition by treatment with MG132 (10 µg/ml, 1 h) on V5-ZC3H11 expression. <b>E.</b> ZC3H11-myc is phosphorylated. Extracts from 5×10<sup>6</sup> cells were incubated with lambda phosphatase, in the presence or absence of inhibitors <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286-Benz1\" target=\"_blank\">[64]</a>. Both the full-length protein (upper panel) and the N-terminal fragment of ZC3H11 (first 128 amino acids; lower panel) are phosphorylated. <b>F.</b> ZC3H11-TAP is localized in the cytoplasm. TAP-tagged protein was detected by immunofluorescence. DAPI - DNA stain, detecting nucleus and kinetoplast (mitochondrial DNA); DIC - differential interference contrast.</p>", "links"=>[], "tags"=>["zc3h11", "induced"], "article_id"=>674829, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.g001", "stats"=>{"downloads"=>0, "page_views"=>11, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Expression_of_ZC3H11_is_induced_by_stress_/674829", "title"=>"Expression of ZC3H11 is induced by stress.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:20:29"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014518"], "description"=>"<p><b>A.</b> The 12mer motif enriched in the 3′-UTRs of transcripts that were enriched in the ZC3H11 bound fraction, as measured by RNASeq. The motif was identified using MotifSampler. <b>B.</b> Purified His-tagged ZC3H11 fragment preparations were separated by SDS-PAGE and either stained with Coomassie (left) or blotted and detected using anti-His antisera (right). Proteins were (1) His-tagged N-terminal 104mer; (2) His-tagged N-terminal 119mer; (3) His-tagged N-terminal 104mer with C70S mutation; (4) His-tagged N-terminal 119mer with C70S mutation. <b>C.</b> The His-tagged ZC3H11 fragments (100 pmol total protein) were incubated with 1 pmol radioactively labelled probe in the presence of 10 mg/ml heparin, then separated by native PAGE. The phosphorimager output is shown. Radioactive RNA probes were: UAU: U(UAU)<sub>7</sub>U; UAUU: (UAUU)<sub>5</sub>UAU; UCU: U(UCU)<sub>7</sub>U. Arrows indicate unbound probe (u), a small UAU or UAUU-specific complex (s1); a larger UAU or UAUU-specific complex (s2); a non-specific complex (n); and aggregates in the well (w). <b>D.</b> The His-tagged N-terminal 104mer of ZC3H11 (100 pmol total protein, Z-104) was incubated with 1 pmol radioactively labelled probe, in the presence of 5 µg/ml heparin, then separated by native PAGE. The phosphorimager output is shown. Radioactive RNA probes were as follows: UAU: U(UAU)<sub>7</sub>U; UAUU: (UAUU)<sub>5</sub>UAU; UCU: U(UCU)<sub>7</sub>U; U: (U)<sub>23</sub>; C: (C)<sub>23</sub>; A: (A)<sub>23</sub>. Arrows indicate unbound probe (u), a UAU or UAUU-specific complex (s1) and a different UCU or poly(U)-specific complex (n). <b>E.</b> The His-tagged N-terminal ZC3H11 104mer (100 pmol total protein) was incubated with 1 pmol radioactively labelled U(UAU)<sub>7</sub>U in the presence of 5 µg/ml heparin and competing oligonucleotides in 5 or 20-fold excess. Remaining details are as in (C). Addition of 10 mg/ml heparin did not affect the result (Supplementary <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286.s002\" target=\"_blank\">Figure S2E</a>).</p>", "links"=>[], "tags"=>["zc3h11", "zinc", "auu"], "article_id"=>674832, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.g002", "stats"=>{"downloads"=>2, "page_views"=>7, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_The_ZC3H11_zinc_finger_can_bind_to_AUU_repeats_/674832", "title"=>"The ZC3H11 zinc finger can bind to AUU repeats.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:20:32"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014519"], "description"=>"<p><b>A.</b> Effect of <i>ZC3H11</i> RNAi on growth of bloodstream forms. Tetracycline was added at day 0, and cells were diluted as required. Cumulative growth curves are shown. Results are for four independent cell lines, immediately after isolation. Results from two experiments are included. In experiment one, three lines were tested over three days of tetracycline treatment. In experiment 2, the same lines plus another were examined for two days with tetracycline. The control is from experiment 1, and shows pooled results for 11 trypanosome lines with RNAi targeting a non-essential gene, growth without tetracycline for three days. Results are shown as arithmetic mean ± standard deviation. <b>B.</b> Effect of <i>ZC3H11</i> RNAi on growth of procyclic forms, cumulative growth curve. Results are shown from triplicate measurements from a line with stem-loop RNAi, as arithmetic mean ± standard deviation. The error bars are not visible because they are smaller than the symbols.</p>", "links"=>[], "tags"=>["depletion", "kills", "bloodstream", "forms"], "article_id"=>674833, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.g003", "stats"=>{"downloads"=>0, "page_views"=>20, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ZC3H11_depletion_kills_bloodstream_forms_but_not_procyclics_/674833", "title"=>"ZC3H11 depletion kills bloodstream forms but not procyclics.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:20:33"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014520"], "description"=>"<p><b>A.</b> Effect of <i>ZC3H11</i> depletion on <i>HSP70</i> mRNA levels in bloodstream forms. <i>HSP70</i> and <i>ZC3H11</i> RNA were detected by Northern blotting after one day of RNAi induction, with the <i>7SL</i> RNA as loading control. <b>B. </b><i>HSP70</i> RNA co-precipitates with myc-tagged ZC3H11. Extracts from trypanosomes expressing no myc-tagged protein (wt), ZC3H11-myc, or ZC3H11-myc with the first cysteine of the zinc finger mutated to serine (C70S), were immunoprecipitated with anti-myc antibody. RNA was purified from the precipitates and analysed by Northern blotting. The blot was probed for <i>HSP70</i>, then reprobed to detect tubulin RNA in order to assess non-specific binding. <b>C.</b> Sequence of the <i>HSP70</i> 3′-UTR amplified from the genome. The underlined A's are alternative polyadenylation sites <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286-Husler1\" target=\"_blank\">[22]</a>. The blue shadowed regions are the AUU repeats. The grey type indicates the primer used to amplify the 5′ and 3′ regions of the 3′-UTR; this sequence is present in both constructs. <b>D.</b> The AUU repeat region is necessary and sufficient for the response to ZC3H11. Stable transgenic bloodstream-form trypanosome cell lines with inducible <i>ZC3H11</i> RNAi and constitutively expressed <i>CAT</i> reporter constructs that integrated into the tubulin locus (pol II transcription) were generated. In the controls, the <i>CAT</i> ORF is flanked by a <i>EP</i> 5′-UTR and either a truncated actin (<i>ACT</i>) 3′-UTR or the full-length <i>ACT</i> 3′-UTR (at the bottom). The other constructs have full length or truncated <i>HSP70</i> UTRs (blue) as indicated. Relative CAT expression levels, with or without RNAi induction (1 day), were determined by Northern blot and CAT activity, and expressed as arithmetic mean ± standard deviation of at least 3 measurements.</p>", "links"=>[], "tags"=>["depletion", "decreases", "mrna", "requires", "au-rich"], "article_id"=>674834, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.g004", "stats"=>{"downloads"=>0, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ZC3H11_depletion_decreases_the_HSP70_mRNA_level_and_this_effect_requires_the_AU_rich_sequence_in_the_3_UTR_/674834", "title"=>"ZC3H11 depletion decreases the <i>HSP70</i> mRNA level and this effect requires the AU-rich sequence in the 3′-UTR.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:20:34"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014521"], "description"=>"<p><b>A.</b> Effects of incubating procyclic cells at 37°C, with or without <i>ZC3H11</i> RNAi. Cells were diluted to 1×10<sup>6</sup>/ml as required to avoid densities above 5×10<sup>6</sup>/ml. Results are for three experiments, expressed as arithmetic mean ± standard deviation. If no error bars are visible, they were smaller than the symbols. <b>B.</b> Recovery of procyclic cells with or without <i>ZC3H11</i> RNAi from a one-hour heat shock at 41°C. On day 0, cells were incubated at 41°C for one hour then returned to 27°C. They were diluted on subsequent days as required. Cells with no heat shock served as controls. Results are for three experiments, expressed as arithmetic mean ± standard deviation. <b>C.</b> Analysis of DNA content of procyclic trypanosomes recovering from heat shock, with and without <i>ZC3H11</i> RNAi by FACS. The growth curve for these particular cells was included in those used to make the graph B. <b>D.</b> Effect of <i>ZC3H11</i> RNAi on heat-shock protein synthesis in procyclic forms. Cells were shocked at 41°C for one hour, then pulsed with [<sup>35</sup>S]-methionine. Labelled proteins were separated by SDS-PAGE and detected by autoradiography. <b>E.</b> Effect of heat shock on total mRNA abundance. RNA was prepared and analysed by Northern blotting after a one-hour heat shock at 41°C. The total mRNA was detected by hybridisation with the spliced leader (present at the 5′-end of each mRNA). The numbers below show the total signal from spliced mRNA (without the <i>SLRNA</i> itself), normalized to ribosomal RNA (measured by methylene blue staining of the blot). <b>F. </b><i>ZC3H11</i> RNAi abolishes the specific stabilization of <i>HSP70</i> mRNA upon heat shock. Northern blots are shown, as in (E) but also including a one-hour incubation at 37°C. The quantitation, normalised to the <i>7SL</i> RNA signal, is the average of 2 independent experiments. <b>G.</b> The UAU-rich region of the <i>HSP70</i> 3′-UTR is able to stablise a reporter mRNA after heat shock. Procyclic trypanosomes expressing <i>CAT</i> reporters with segments of the <i>HSP70</i> 3′-UTR were incubated at 41°C for one hour, then RNA was prepared and analysed by Northern blotting. Constructs contained either full-length <i>HSP70</i> 3′-UTR or the fragments “delAU” or “onlyAU” (<a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat-1003286-g004\" target=\"_blank\">Figure 4</a>) and the reporter with full-length actin 3′-UTR served as control. For each reporter, <i>CAT</i> RNA levels were quantified relative to the non-heat shock level and normalized using the <i>7SL</i> signal.</p>", "links"=>[], "tags"=>["procyclic", "trypanosomes"], "article_id"=>674835, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.g005", "stats"=>{"downloads"=>0, "page_views"=>12, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_ZC3H11_is_required_for_recovery_of_procyclic_trypanosomes_from_heat_shock_/674835", "title"=>"ZC3H11 is required for recovery of procyclic trypanosomes from heat shock.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:20:35"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014522"], "description"=>"<p><b>A.</b> Constructs used for the tethering experiments. Above: permanent cell lines were made with constitutive production of a <i>CAT</i> reporter mRNA, with or without five “boxB” recognition sites in the 3′-UTRs. Below: additional cell lines were generated with tetracycline-inducible expression of ZC3H11 (full length or fragments) with an N-terminal lambda-N peptide and C-terminal myc tag. <b>B.</b> Expression of ZC3H11 fusion proteins. Western blotting, using anti-myc, with anti-aldolase or a cross-reacting non-specific band (*) as loading control (1×10<sup>7</sup> cells per lane). <b>C.</b> Expression of CAT in cells with or without inducible expression of lambda-N-ZC3H11-myc, or the fragments. RNA and protein extracts were prepared from cells with or without tetracycline treatment to induce fusion protein expression (100 ng/ml, 24 h). RNA was measured by Northern blotting and CAT enzyme activity was assayed. Results are arithmetic mean ± standard deviation of at least 3 measurements. The increase of CAT with lambda-N-ZC3H11-myc without tetracycline addition is probably due to leaky expression (see B).</p>", "links"=>[], "tags"=>["zc3h11", "abundance"], "article_id"=>674836, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.g006", "stats"=>{"downloads"=>1, "page_views"=>23, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Tethering_of_ZC3H11_increases_the_abundance_of_a_reporter_mRNA_/674836", "title"=>"Tethering of ZC3H11 increases the abundance of a reporter mRNA.", "pos_in_sequence"=>0, "defined_type"=>1, "published_date"=>"2013-04-04 01:20:36"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014523"], "description"=>"<p>The Table includes all mRNAs that were at least 3-fold enriched in the ZC3H11 bound fraction, with more than 40 reads in the bound fraction and more than10 reads per million in the unbound fraction. The full lists are in Supplementary <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286.s006\" target=\"_blank\">Table S1</a>. The genes are grouped according to predicted protein function. All RNASeq results were normalised to reads per million per kilobase (rpkm) before the ratios were calculated. PC bind: Ratio of eluate to flow-through in the binding experiment. “Description” is the functional classification in TriTrypDB, with some additions and modifications. PC HS Seq: RNA rpm for procyclics heated to 41°C for 1 h, relative to procyclics kept at 27°C. PC HS RNAi: RNA read counts per million in procyclics with <i>ZC3H11</i> RNAi, heated to 41°C for 1 h, divided by the read counts in wild-type procyclics heated to 41°C;</p>*<p>Northern blot result between 1× and 1.5× (Supplementary <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286.s005\" target=\"_blank\">Figure S5</a>);</p>§<p>Northern or published microarray result 5–6× <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286-Kramer1\" target=\"_blank\">[17]</a>. BS RNAi Seq: effect of RNAi targeting <i>ZC3H11</i> in bloodstream forms, relative to wild-type. “(AUU)<sub>3</sub>”: “yes” indicates the presence of (at least) the 12mer AUUAUUAUUAUU in the 3′-UTR, (yes) is a perfectly-matching 11mer. PPIase = peptidyl prolyl cis-trans isomerase; TM = trans-membrane domain, DUF866 = domain of unknown function. For multi-copy genes only one member is shown. They are <i>HSP83</i> (Tb917.10.10890-10980), <i>HSP60</i> (Tb927.10.6400 and 6510), and <i>HSP70</i>.</p>", "links"=>[], "tags"=>["mrna", "targets"], "article_id"=>674837, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.t001", "stats"=>{"downloads"=>8, "page_views"=>18, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Possible_mRNA_targets_of_ZC3H11_/674837", "title"=>"Possible mRNA targets of ZC3H11.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-04-04 01:20:37"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014524"], "description"=>"<p>The list shows mRNAs with predicted functions that were found to be increased by RNASeq (Seq) and in a previous microarray analysis (MA); 54 additional ORFs encoding proteins of unknown function were also increased in both analyses. BS/PC shows the ratio of mRNA in bloodstream forms relative to procyclic forms according to Siegel et al <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286-Siegel1\" target=\"_blank\">[69]</a>. The full list is in Supplementary <a href=\"http://www.plospathogens.org/article/info:doi/10.1371/journal.ppat.1003286#ppat.1003286.s006\" target=\"_blank\">Table S1</a>, sheet 4. The raw microarray data include values for duplicate spots of each gene; in this table the higher value for regulation has been quoted.</p>", "links"=>[], "tags"=>["mrna", "procyclic"], "article_id"=>674838, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>"https://dx.doi.org/10.1371/journal.ppat.1003286.t002", "stats"=>{"downloads"=>14, "page_views"=>10, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Genes_with_increased_mRNA_after_heat_shock_of_procyclic_forms_/674838", "title"=>"Genes with increased mRNA after heat shock of procyclic forms.", "pos_in_sequence"=>0, "defined_type"=>3, "published_date"=>"2013-04-04 01:20:38"}
  • {"files"=>["https://ndownloader.figshare.com/files/1014527", "https://ndownloader.figshare.com/files/1014529", "https://ndownloader.figshare.com/files/1014534", "https://ndownloader.figshare.com/files/1014538", "https://ndownloader.figshare.com/files/1014541", "https://ndownloader.figshare.com/files/1014543", "https://ndownloader.figshare.com/files/1014545"], "description"=>"<div><p>In most organisms, the heat-shock response involves increased heat-shock gene transcription. In Kinetoplastid protists, however, virtually all control of gene expression is post-transcriptional. Correspondingly, <i>Trypanosoma brucei</i> heat-shock protein 70 (HSP70) synthesis after heat shock depends on regulation of <i>HSP70</i> mRNA turnover. We here show that the <i>T. brucei</i> CCCH zinc finger protein ZC3H11 is a post-transcriptional regulator of trypanosome chaperone mRNAs. ZC3H11 is essential in bloodstream-form trypanosomes and for recovery of insect-form trypanosomes from heat shock. ZC3H11 binds to mRNAs encoding heat-shock protein homologues, with clear specificity for the subset of trypanosome chaperones that is required for protein refolding. In procyclic forms, ZC3H11 was required for stabilisation of target chaperone-encoding mRNAs after heat shock, and the <i>HSP70</i> mRNA was also decreased upon ZC3H11 depletion in bloodstream forms. Many mRNAs bound to ZC3H11 have a consensus AUU repeat motif in the 3′-untranslated region. ZC3H11 bound preferentially to AUU repeats <i>in vitro</i>, and ZC3H11 regulation of <i>HSP70</i> mRNA in bloodstream forms depended on its AUU repeat region. Tethering of ZC3H11 to a reporter mRNA increased reporter expression, showing that it is capable of actively stabilizing an mRNA. These results show that expression of trypanosome heat-shock genes is controlled by a specific RNA-protein interaction. They also show that heat-shock-induced chaperone expression in procyclic trypanosome enhances parasite survival at elevated temperatures.</p> </div>", "links"=>[], "tags"=>["trypanosome", "zinc"], "article_id"=>674840, "categories"=>["Molecular Biology", "Cell Biology", "Microbiology"], "users"=>["Dorothea Droll", "Igor Minia", "Abeer Fadda", "Aditi Singh", "Mhairi Stewart", "Rafael Queiroz", "Christine Clayton"], "doi"=>["https://dx.doi.org/10.1371/journal.ppat.1003286.s001", "https://dx.doi.org/10.1371/journal.ppat.1003286.s002", "https://dx.doi.org/10.1371/journal.ppat.1003286.s003", "https://dx.doi.org/10.1371/journal.ppat.1003286.s004", "https://dx.doi.org/10.1371/journal.ppat.1003286.s005", "https://dx.doi.org/10.1371/journal.ppat.1003286.s006", "https://dx.doi.org/10.1371/journal.ppat.1003286.s007"], "stats"=>{"downloads"=>6, "page_views"=>32, "likes"=>0}, "figshare_url"=>"https://figshare.com/articles/_Post_Transcriptional_Regulation_of_the_Trypanosome_Heat_Shock_Response_by_a_Zinc_Finger_Protein_/674840", "title"=>"Post-Transcriptional Regulation of the Trypanosome Heat Shock Response by a Zinc Finger Protein", "pos_in_sequence"=>0, "defined_type"=>4, "published_date"=>"2013-04-04 01:20:40"}

PMC Usage Stats | Further Information

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Relative Metric

{"start_date"=>"2013-01-01T00:00:00Z", "end_date"=>"2013-12-31T00:00:00Z", "subject_areas"=>[{"subject_area"=>"/Biology and life sciences/Biochemistry", "average_usage"=>[266, 468, 593, 703, 804, 903, 993, 1084, 1171, 1256, 1339, 1422, 1492]}, {"subject_area"=>"/Biology and life sciences/Cell biology", "average_usage"=>[272, 472, 600, 713, 815, 911, 1004, 1094, 1185, 1273, 1358, 1441]}, {"subject_area"=>"/Biology and life sciences/Molecular biology", "average_usage"=>[272, 466, 589, 702, 806, 903, 995, 1086, 1176, 1258, 1347, 1422, 1493]}]}
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Net::HTTPTooManyRequests

Source
Scopus
Time
2019-08-27 18:06:09 UTC
Target URL
https://api.elsevier.com/content/search/index:SCOPUS?query=DOI(10.1371%2Fjournal.ppat.1003286)
Trace

/app/models/concerns/networkable.rb:21:in `get_result'
/app/models/source.rb:165:in `get_data'
/app/models/retrieval_status.rb:47:in `perform_get_data'
/app/jobs/source_job.rb:52:in `block (2 levels) in perform'
/app/jobs/source_job.rb:51:in `block in perform'
/app/jobs/source_job.rb:35:in `each'
/app/jobs/source_job.rb:35:in `perform'