RNA-cleaving properties of human apurinic/apyrimidinic endonuclease 1 (APE1).
Identifieur interne : 000D35 ( PubMed/Corpus ); précédent : 000D34; suivant : 000D36RNA-cleaving properties of human apurinic/apyrimidinic endonuclease 1 (APE1).
Auteurs : Wan-Cheol Kim ; Dustin King ; Chow H. LeeSource :
- International journal of biochemistry and molecular biology [ 2152-4114 ] ; 2010.
Abstract
We have recently identified apurinic/apyrimidinic endonuclease 1 (APE1) as an endoribonuclease that cleaves c-myc mRNA in vitro and regulates c-myc mRNA levels and half-life in cells. This study was undertaken to further unravel the RNA-cleaving properties of APE1. Here, we show that APE1 cleaves RNA in the absence of divalent metal ions and, at 2 mM, Zn(2+), Ni(2+), Cu(2+), or Co(2+) inhibited the endoribonuclease activity of APE1. APE1 is able to cleave CD44 mRNA, microRNAs (miR-21, miR-10b), and three RNA components of SARS-corona virus (orf1b, orf3, spike) suggesting that, when challenged, it can cleave any RNAs in vitro. APE1 does not cleave strong doublestranded regions of RNA and it has a strong preference for 3' of pyrimidine, especially towards UA, CA, and UG sites at single-stranded or weakly paired regions. It also cleaves RNA weakly at UC, CU, AC, and AU sites in single-stranded or weakly paired regions. Finally, we found that APE1 can reduce the ability of the Dicer enzyme to process premiRNAs in vitro. Overall, this study has revealed some previously unknown biochemical properties of APE1 which has implications for its role in vivo.
PubMed: 21968700
Links to Exploration step
pubmed:21968700Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">RNA-cleaving properties of human apurinic/apyrimidinic endonuclease 1 (APE1).</title>
<author><name sortKey="Kim, Wan Cheol" sort="Kim, Wan Cheol" uniqKey="Kim W" first="Wan-Cheol" last="Kim">Wan-Cheol Kim</name>
<affiliation><nlm:affiliation>Chemistry Program, University of Northern British Columbia, 3333 University Way Prince George, BC V2N 4Z9 Canada.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="King, Dustin" sort="King, Dustin" uniqKey="King D" first="Dustin" last="King">Dustin King</name>
</author>
<author><name sortKey="Lee, Chow H" sort="Lee, Chow H" uniqKey="Lee C" first="Chow H" last="Lee">Chow H. Lee</name>
</author>
</titleStmt>
<publicationStmt><idno type="wicri:source">PubMed</idno>
<date when="2010">2010</date>
<idno type="RBID">pubmed:21968700</idno>
<idno type="pmid">21968700</idno>
<idno type="wicri:Area/PubMed/Corpus">000D35</idno>
<idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000D35</idno>
</publicationStmt>
<sourceDesc><biblStruct><analytic><title xml:lang="en">RNA-cleaving properties of human apurinic/apyrimidinic endonuclease 1 (APE1).</title>
<author><name sortKey="Kim, Wan Cheol" sort="Kim, Wan Cheol" uniqKey="Kim W" first="Wan-Cheol" last="Kim">Wan-Cheol Kim</name>
<affiliation><nlm:affiliation>Chemistry Program, University of Northern British Columbia, 3333 University Way Prince George, BC V2N 4Z9 Canada.</nlm:affiliation>
</affiliation>
</author>
<author><name sortKey="King, Dustin" sort="King, Dustin" uniqKey="King D" first="Dustin" last="King">Dustin King</name>
</author>
<author><name sortKey="Lee, Chow H" sort="Lee, Chow H" uniqKey="Lee C" first="Chow H" last="Lee">Chow H. Lee</name>
</author>
</analytic>
<series><title level="j">International journal of biochemistry and molecular biology</title>
<idno type="ISSN">2152-4114</idno>
<imprint><date when="2010" type="published">2010</date>
</imprint>
</series>
</biblStruct>
</sourceDesc>
</fileDesc>
<profileDesc><textClass></textClass>
</profileDesc>
</teiHeader>
<front><div type="abstract" xml:lang="en">We have recently identified apurinic/apyrimidinic endonuclease 1 (APE1) as an endoribonuclease that cleaves c-myc mRNA in vitro and regulates c-myc mRNA levels and half-life in cells. This study was undertaken to further unravel the RNA-cleaving properties of APE1. Here, we show that APE1 cleaves RNA in the absence of divalent metal ions and, at 2 mM, Zn(2+), Ni(2+), Cu(2+), or Co(2+) inhibited the endoribonuclease activity of APE1. APE1 is able to cleave CD44 mRNA, microRNAs (miR-21, miR-10b), and three RNA components of SARS-corona virus (orf1b, orf3, spike) suggesting that, when challenged, it can cleave any RNAs in vitro. APE1 does not cleave strong doublestranded regions of RNA and it has a strong preference for 3' of pyrimidine, especially towards UA, CA, and UG sites at single-stranded or weakly paired regions. It also cleaves RNA weakly at UC, CU, AC, and AU sites in single-stranded or weakly paired regions. Finally, we found that APE1 can reduce the ability of the Dicer enzyme to process premiRNAs in vitro. Overall, this study has revealed some previously unknown biochemical properties of APE1 which has implications for its role in vivo.</div>
</front>
</TEI>
<pubmed><MedlineCitation Status="Publisher" Owner="NLM"><PMID Version="1">21968700</PMID>
<DateRevised><Year>2019</Year>
<Month>11</Month>
<Day>20</Day>
</DateRevised>
<Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Print">2152-4114</ISSN>
<JournalIssue CitedMedium="Print"><Volume>1</Volume>
<Issue>1</Issue>
<PubDate><Year>2010</Year>
</PubDate>
</JournalIssue>
<Title>International journal of biochemistry and molecular biology</Title>
<ISOAbbreviation>Int J Biochem Mol Biol</ISOAbbreviation>
</Journal>
<ArticleTitle>RNA-cleaving properties of human apurinic/apyrimidinic endonuclease 1 (APE1).</ArticleTitle>
<Pagination><MedlinePgn>12-25</MedlinePgn>
</Pagination>
<Abstract><AbstractText>We have recently identified apurinic/apyrimidinic endonuclease 1 (APE1) as an endoribonuclease that cleaves c-myc mRNA in vitro and regulates c-myc mRNA levels and half-life in cells. This study was undertaken to further unravel the RNA-cleaving properties of APE1. Here, we show that APE1 cleaves RNA in the absence of divalent metal ions and, at 2 mM, Zn(2+), Ni(2+), Cu(2+), or Co(2+) inhibited the endoribonuclease activity of APE1. APE1 is able to cleave CD44 mRNA, microRNAs (miR-21, miR-10b), and three RNA components of SARS-corona virus (orf1b, orf3, spike) suggesting that, when challenged, it can cleave any RNAs in vitro. APE1 does not cleave strong doublestranded regions of RNA and it has a strong preference for 3' of pyrimidine, especially towards UA, CA, and UG sites at single-stranded or weakly paired regions. It also cleaves RNA weakly at UC, CU, AC, and AU sites in single-stranded or weakly paired regions. Finally, we found that APE1 can reduce the ability of the Dicer enzyme to process premiRNAs in vitro. Overall, this study has revealed some previously unknown biochemical properties of APE1 which has implications for its role in vivo.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kim</LastName>
<ForeName>Wan-Cheol</ForeName>
<Initials>WC</Initials>
<AffiliationInfo><Affiliation>Chemistry Program, University of Northern British Columbia, 3333 University Way Prince George, BC V2N 4Z9 Canada.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>King</LastName>
<ForeName>Dustin</ForeName>
<Initials>D</Initials>
</Author>
<Author ValidYN="Y"><LastName>Lee</LastName>
<ForeName>Chow H</ForeName>
<Initials>CH</Initials>
</Author>
</AuthorList>
<Language>eng</Language>
<PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType>
</PublicationTypeList>
<ArticleDate DateType="Electronic"><Year>2010</Year>
<Month>03</Month>
<Day>10</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Int J Biochem Mol Biol</MedlineTA>
<NlmUniqueID>101532076</NlmUniqueID>
<ISSNLinking>2152-4114</ISSNLinking>
</MedlineJournalInfo>
</MedlineCitation>
<PubmedData><History><PubMedPubDate PubStatus="received"><Year>2010</Year>
<Month>02</Month>
<Day>11</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted"><Year>2010</Year>
<Month>03</Month>
<Day>03</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez"><Year>2011</Year>
<Month>10</Month>
<Day>5</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed"><Year>2010</Year>
<Month>1</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline"><Year>2010</Year>
<Month>1</Month>
<Day>1</Day>
<Hour>0</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList><ArticleId IdType="pubmed">21968700</ArticleId>
<ArticleId IdType="pmc">PMC3180037</ArticleId>
</ArticleIdList>
<ReferenceList><Reference><Citation>Mol Cell Biol. 1994 Mar;14(3):2119-28</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8114742</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 1992 Apr;6(4):642-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1559612</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Chem Rev. 1998 May 7;98(3):1045-1066</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11848924</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1998 Nov 13;273(46):30360-5</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9804799</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 1994;63:915-48</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7979257</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nat Struct Mol Biol. 2008 Nov;15(11):1228-31</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18953336</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 1999 Jul 9;290(2):447-57</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10390343</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2005 Feb 4;345(5):1003-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15644200</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Genes Dev. 1997 Mar 1;11(5):558-70</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9119221</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mutat Res. 2001 May 10;485(4):283-307</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11585362</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Pharm Res. 2003 Sep;20(9):1389-93</Citation>
<ArticleIdList><ArticleId IdType="pubmed">14567632</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Antiviral Res. 2005 Feb;65(2):69-78</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15708633</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 2003 May 16;278(20):18241-8</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12604611</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Science. 2003 May 30;300(5624):1399-404</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12730501</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2005 Jun 1;24(11):1988-98</Citation>
<ArticleIdList><ArticleId IdType="pubmed">15889141</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2008 Dec;28(23):7066-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18809583</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1991 Nov 11;19(21):5907-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1719484</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 2006 Apr 5;25(7):1456-68</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16541107</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2009 Mar;29(6):1442-51</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19124611</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nature. 2000 Jan 27;403(6768):451-6</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10667800</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>FEBS Lett. 2007 Dec 22;581(30):5774-80</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18037383</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2002 Feb 1;30(3):823-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11809897</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1995 Jul 7;270(27):16002-7</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7608159</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2008 May 23;379(1):17-27</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18439621</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 1997 May;17(5):2698-707</Citation>
<ArticleIdList><ArticleId IdType="pubmed">9111340</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>RNA. 2008 Feb;14(2):284-96</Citation>
<ArticleIdList><ArticleId IdType="pubmed">18073345</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Annu Rev Biochem. 2003;72:291-336</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12626338</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Oncogene. 1993 Jul;8(7):1921-9</Citation>
<ArticleIdList><ArticleId IdType="pubmed">8510935</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Mol Cell Biol. 2009 Apr;29(7):1834-54</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19188445</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Biol Chem. 1981 Apr 10;256(7):3405-14</Citation>
<ArticleIdList><ArticleId IdType="pubmed">6259165</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1992 Sep;11(9):3323-35</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1380454</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Biopolymers. 1998;48(2-3):181-95</Citation>
<ArticleIdList><ArticleId IdType="pubmed">10333745</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Mol Biol. 2001 Apr 6;307(4):1023-34</Citation>
<ArticleIdList><ArticleId IdType="pubmed">11286553</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>J Cell Biochem. 2006 Jun 1;98(3):519-37</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16317762</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2009 Jul;37(12):3946-58</Citation>
<ArticleIdList><ArticleId IdType="pubmed">19401441</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1987 Nov 25;15(22):9109-28</Citation>
<ArticleIdList><ArticleId IdType="pubmed">2446263</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>EMBO J. 1992 Feb;11(2):653-65</Citation>
<ArticleIdList><ArticleId IdType="pubmed">1537340</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Proteins. 2007 Jul 1;68(1):313-23</Citation>
<ArticleIdList><ArticleId IdType="pubmed">17427952</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 2003 Jul 1;31(13):3406-15</Citation>
<ArticleIdList><ArticleId IdType="pubmed">12824337</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Nucleic Acids Res. 1995 May 11;23(9):1544-50</Citation>
<ArticleIdList><ArticleId IdType="pubmed">7784208</ArticleId>
</ArticleIdList>
</Reference>
<Reference><Citation>Toxicol Lett. 2006 Oct 25;166(3):237-47</Citation>
<ArticleIdList><ArticleId IdType="pubmed">16938414</ArticleId>
</ArticleIdList>
</Reference>
</ReferenceList>
</PubmedData>
</pubmed>
</record>
Pour manipuler ce document sous Unix (Dilib)
EXPLOR_STEP=$WICRI_ROOT/Wicri/Sante/explor/CovidV2/Data/PubMed/Corpus
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000D35 | SxmlIndent | more
Ou
HfdSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd -nk 000D35 | SxmlIndent | more
Pour mettre un lien sur cette page dans le réseau Wicri
{{Explor lien |wiki= Wicri/Sante |area= CovidV2 |flux= PubMed |étape= Corpus |type= RBID |clé= pubmed:21968700 |texte= RNA-cleaving properties of human apurinic/apyrimidinic endonuclease 1 (APE1). }}
Pour générer des pages wiki
HfdIndexSelect -h $EXPLOR_AREA/Data/PubMed/Corpus/RBID.i -Sk "pubmed:21968700" \ | HfdSelect -Kh $EXPLOR_AREA/Data/PubMed/Corpus/biblio.hfd \ | NlmPubMed2Wicri -a CovidV2
![]() | This area was generated with Dilib version V0.6.33. | ![]() |