Reactivity and Specificity of RNase T1, RNase A, and RNase H toward Oligonucleotides of RNA Containing 8-Oxo-7,8-dihydroguanosine.
Identifieur interne : 000921 ( PubMed/Corpus ); précédent : 000920; suivant : 000922Reactivity and Specificity of RNase T1, RNase A, and RNase H toward Oligonucleotides of RNA Containing 8-Oxo-7,8-dihydroguanosine.
Auteurs : Cassandra Herbert ; Yannick Kokouvi Dzowo ; Anthony Urban ; Courtney N. Kiggins ; Marino J E. ResendizSource :
- Biochemistry [ 1520-4995 ] ; 2018.
English descriptors
- KwdEn :
- Circular Dichroism, Guanosine (analogs & derivatives), Guanosine (chemistry), Guanosine (genetics), Humans, Oligonucleotides (chemistry), Oligonucleotides (genetics), Oxidative Stress (genetics), RNA (chemistry), RNA (genetics), Ribonuclease H (chemistry), Ribonuclease H (genetics), Ribonuclease T1 (chemistry), Ribonuclease T1 (genetics), Ribonuclease, Pancreatic (chemistry), Ribonuclease, Pancreatic (genetics), Ribonucleases (chemistry), Ribonucleases (genetics), Substrate Specificity.
- MESH :
- chemical , analogs & derivatives : Guanosine.
- chemical , chemistry : Guanosine, Oligonucleotides, RNA, Ribonuclease H, Ribonuclease T1, Ribonuclease, Pancreatic, Ribonucleases.
- chemical , genetics : Guanosine, Oligonucleotides, RNA, Ribonuclease H, Ribonuclease T1, Ribonuclease, Pancreatic, Ribonucleases.
- genetics : Oxidative Stress.
- Circular Dichroism, Humans, Substrate Specificity.
Abstract
Understanding how oxidatively damaged RNA interacts with ribonucleases is important because of its proposed role in the development and progression of disease. Thus, understanding structural aspects of RNA containing lesions generated under oxidative stress, as well as its interactions with other biopolymers, is fundamental. We explored the reactivity of RNase A, RNase T1, and RNase H toward oligonucleotides of RNA containing 8-oxo-7,8-dihydroguanosine (8oxoG). This is the first example that addresses this relationship and will be useful for understanding (1) how these RNases can be used to characterize the structural impact that this lesion has on RNA and (2) how oxidatively modified RNA may be handled intracellularly. 8-OxoG was incorporated into 10-16-mers of RNA, and its reactivity with each ribonuclease was assessed via electrophoretic analyses, circular dichroism, and the use of other C8-purine-modified analogues (8-bromoguanosine, 8-methoxyguanosine, and 8-oxoadenosine). RNase T1 does not recognize sites containing 8-oxoG, while RNase A recognizes and cleaves RNA at positions containing this lesion while differentiating if it is involved in H-bonding. The selectivity of RNase A followed the order C > 8-oxoG ≈ U. In addition, isothermal titration calorimetry showed that an 8-oxoG-C3'-methylphosphate derivative can inhibit RNase A activity. Cleavage patterns obtained from RNase H displayed changes in reactivity in a sequence- and concentration-dependent manner and displayed recognition at sites containing the modification in some cases. These data will aid in understanding how this modification affects reactivity with ribonucleases and will enable the characterization of global and local structural changes in oxidatively damaged RNA.
DOI: 10.1021/acs.biochem.8b00277
PubMed: 29683663
Links to Exploration step
pubmed:29683663Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Reactivity and Specificity of RNase T<sub>1</sub>, RNase A, and RNase H toward Oligonucleotides of RNA Containing 8-Oxo-7,8-dihydroguanosine.</title><author><name sortKey="Herbert, Cassandra" sort="Herbert, Cassandra" uniqKey="Herbert C" first="Cassandra" last="Herbert">Cassandra Herbert</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Dzowo, Yannick Kokouvi" sort="Dzowo, Yannick Kokouvi" uniqKey="Dzowo Y" first="Yannick Kokouvi" last="Dzowo">Yannick Kokouvi Dzowo</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Urban, Anthony" sort="Urban, Anthony" uniqKey="Urban A" first="Anthony" last="Urban">Anthony Urban</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Kiggins, Courtney N" sort="Kiggins, Courtney N" uniqKey="Kiggins C" first="Courtney N" last="Kiggins">Courtney N. Kiggins</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Resendiz, Marino J E" sort="Resendiz, Marino J E" uniqKey="Resendiz M" first="Marino J E" last="Resendiz">Marino J E. Resendiz</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2018">2018</date><idno type="RBID">pubmed:29683663</idno><idno type="pmid">29683663</idno><idno type="doi">10.1021/acs.biochem.8b00277</idno><idno type="wicri:Area/PubMed/Corpus">000921</idno><idno type="wicri:explorRef" wicri:stream="PubMed" wicri:step="Corpus" wicri:corpus="PubMed">000921</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Reactivity and Specificity of RNase T<sub>1</sub>, RNase A, and RNase H toward Oligonucleotides of RNA Containing 8-Oxo-7,8-dihydroguanosine.</title><author><name sortKey="Herbert, Cassandra" sort="Herbert, Cassandra" uniqKey="Herbert C" first="Cassandra" last="Herbert">Cassandra Herbert</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Dzowo, Yannick Kokouvi" sort="Dzowo, Yannick Kokouvi" uniqKey="Dzowo Y" first="Yannick Kokouvi" last="Dzowo">Yannick Kokouvi Dzowo</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Urban, Anthony" sort="Urban, Anthony" uniqKey="Urban A" first="Anthony" last="Urban">Anthony Urban</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Kiggins, Courtney N" sort="Kiggins, Courtney N" uniqKey="Kiggins C" first="Courtney N" last="Kiggins">Courtney N. Kiggins</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author><author><name sortKey="Resendiz, Marino J E" sort="Resendiz, Marino J E" uniqKey="Resendiz M" first="Marino J E" last="Resendiz">Marino J E. Resendiz</name><affiliation><nlm:affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</nlm:affiliation></affiliation></author></analytic><series><title level="j">Biochemistry</title><idno type="eISSN">1520-4995</idno><imprint><date when="2018" type="published">2018</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Circular Dichroism</term><term>Guanosine (analogs & derivatives)</term><term>Guanosine (chemistry)</term><term>Guanosine (genetics)</term><term>Humans</term><term>Oligonucleotides (chemistry)</term><term>Oligonucleotides (genetics)</term><term>Oxidative Stress (genetics)</term><term>RNA (chemistry)</term><term>RNA (genetics)</term><term>Ribonuclease H (chemistry)</term><term>Ribonuclease H (genetics)</term><term>Ribonuclease T1 (chemistry)</term><term>Ribonuclease T1 (genetics)</term><term>Ribonuclease, Pancreatic (chemistry)</term><term>Ribonuclease, Pancreatic (genetics)</term><term>Ribonucleases (chemistry)</term><term>Ribonucleases (genetics)</term><term>Substrate Specificity</term></keywords><keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Guanosine</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Guanosine</term><term>Oligonucleotides</term><term>RNA</term><term>Ribonuclease H</term><term>Ribonuclease T1</term><term>Ribonuclease, Pancreatic</term><term>Ribonucleases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Guanosine</term><term>Oligonucleotides</term><term>RNA</term><term>Ribonuclease H</term><term>Ribonuclease T1</term><term>Ribonuclease, Pancreatic</term><term>Ribonucleases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Oxidative Stress</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Circular Dichroism</term><term>Humans</term><term>Substrate Specificity</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Understanding how oxidatively damaged RNA interacts with ribonucleases is important because of its proposed role in the development and progression of disease. Thus, understanding structural aspects of RNA containing lesions generated under oxidative stress, as well as its interactions with other biopolymers, is fundamental. We explored the reactivity of RNase A, RNase T<sub>1</sub>, and RNase H toward oligonucleotides of RNA containing 8-oxo-7,8-dihydroguanosine (8oxoG). This is the first example that addresses this relationship and will be useful for understanding (1) how these RNases can be used to characterize the structural impact that this lesion has on RNA and (2) how oxidatively modified RNA may be handled intracellularly. 8-OxoG was incorporated into 10-16-mers of RNA, and its reactivity with each ribonuclease was assessed via electrophoretic analyses, circular dichroism, and the use of other C8-purine-modified analogues (8-bromoguanosine, 8-methoxyguanosine, and 8-oxoadenosine). RNase T<sub>1</sub> does not recognize sites containing 8-oxoG, while RNase A recognizes and cleaves RNA at positions containing this lesion while differentiating if it is involved in H-bonding. The selectivity of RNase A followed the order C > 8-oxoG ≈ U. In addition, isothermal titration calorimetry showed that an 8-oxoG-C3'-methylphosphate derivative can inhibit RNase A activity. Cleavage patterns obtained from RNase H displayed changes in reactivity in a sequence- and concentration-dependent manner and displayed recognition at sites containing the modification in some cases. These data will aid in understanding how this modification affects reactivity with ribonucleases and will enable the characterization of global and local structural changes in oxidatively damaged RNA.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">29683663</PMID><DateCompleted><Year>2018</Year><Month>09</Month><Day>13</Day></DateCompleted><DateRevised><Year>2018</Year><Month>09</Month><Day>13</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1520-4995</ISSN><JournalIssue CitedMedium="Internet"><Volume>57</Volume><Issue>20</Issue><PubDate><Year>2018</Year><Month>05</Month><Day>22</Day></PubDate></JournalIssue><Title>Biochemistry</Title><ISOAbbreviation>Biochemistry</ISOAbbreviation></Journal><ArticleTitle>Reactivity and Specificity of RNase T<sub>1</sub>, RNase A, and RNase H toward Oligonucleotides of RNA Containing 8-Oxo-7,8-dihydroguanosine.</ArticleTitle><Pagination><MedlinePgn>2971-2983</MedlinePgn></Pagination><ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.8b00277</ELocationID><Abstract><AbstractText>Understanding how oxidatively damaged RNA interacts with ribonucleases is important because of its proposed role in the development and progression of disease. Thus, understanding structural aspects of RNA containing lesions generated under oxidative stress, as well as its interactions with other biopolymers, is fundamental. We explored the reactivity of RNase A, RNase T<sub>1</sub>, and RNase H toward oligonucleotides of RNA containing 8-oxo-7,8-dihydroguanosine (8oxoG). This is the first example that addresses this relationship and will be useful for understanding (1) how these RNases can be used to characterize the structural impact that this lesion has on RNA and (2) how oxidatively modified RNA may be handled intracellularly. 8-OxoG was incorporated into 10-16-mers of RNA, and its reactivity with each ribonuclease was assessed via electrophoretic analyses, circular dichroism, and the use of other C8-purine-modified analogues (8-bromoguanosine, 8-methoxyguanosine, and 8-oxoadenosine). RNase T<sub>1</sub> does not recognize sites containing 8-oxoG, while RNase A recognizes and cleaves RNA at positions containing this lesion while differentiating if it is involved in H-bonding. The selectivity of RNase A followed the order C > 8-oxoG ≈ U. In addition, isothermal titration calorimetry showed that an 8-oxoG-C3'-methylphosphate derivative can inhibit RNase A activity. Cleavage patterns obtained from RNase H displayed changes in reactivity in a sequence- and concentration-dependent manner and displayed recognition at sites containing the modification in some cases. These data will aid in understanding how this modification affects reactivity with ribonucleases and will enable the characterization of global and local structural changes in oxidatively damaged RNA.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Herbert</LastName><ForeName>Cassandra</ForeName><Initials>C</Initials><AffiliationInfo><Affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dzowo</LastName><ForeName>Yannick Kokouvi</ForeName><Initials>YK</Initials><AffiliationInfo><Affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Urban</LastName><ForeName>Anthony</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Kiggins</LastName><ForeName>Courtney N</ForeName><Initials>CN</Initials><AffiliationInfo><Affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Resendiz</LastName><ForeName>Marino J E</ForeName><Initials>MJE</Initials><Identifier Source="ORCID">0000-0001-5631-2722</Identifier><AffiliationInfo><Affiliation>Department of Chemistry , University of Colorado Denver , Science Building, 1151 Arapahoe Street , Denver , Colorado 80204 , United States.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2018</Year><Month>05</Month><Day>04</Day></ArticleDate></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Biochemistry</MedlineTA><NlmUniqueID>0370623</NlmUniqueID><ISSNLinking>0006-2960</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D009841">Oligonucleotides</NameOfSubstance></Chemical><Chemical><RegistryNumber>12133JR80S</RegistryNumber><NameOfSubstance UI="D006151">Guanosine</NameOfSubstance></Chemical><Chemical><RegistryNumber>3868-31-3</RegistryNumber><NameOfSubstance UI="C046215">8-hydroxyguanosine</NameOfSubstance></Chemical><Chemical><RegistryNumber>63231-63-0</RegistryNumber><NameOfSubstance UI="D012313">RNA</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.-</RegistryNumber><NameOfSubstance UI="D012260">Ribonucleases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.26.4</RegistryNumber><NameOfSubstance UI="D016914">Ribonuclease H</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.27.3</RegistryNumber><NameOfSubstance UI="D006163">Ribonuclease T1</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 3.1.27.5</RegistryNumber><NameOfSubstance UI="D012259">Ribonuclease, Pancreatic</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D002942" MajorTopicYN="N">Circular Dichroism</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006151" MajorTopicYN="N">Guanosine</DescriptorName><QualifierName UI="Q000031" MajorTopicYN="N">analogs & derivatives</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009841" MajorTopicYN="N">Oligonucleotides</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012313" MajorTopicYN="N">RNA</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016914" MajorTopicYN="N">Ribonuclease H</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006163" MajorTopicYN="N">Ribonuclease T1</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012259" MajorTopicYN="N">Ribonuclease, Pancreatic</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012260" MajorTopicYN="N">Ribonucleases</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013379" MajorTopicYN="N">Substrate Specificity</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2018</Year><Month>4</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2018</Year><Month>9</Month><Day>14</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2018</Year><Month>4</Month><Day>24</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">29683663</ArticleId><ArticleId IdType="doi">10.1021/acs.biochem.8b00277</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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