IronSulferCluV1, Main, Exploration, bibRecord, 000005

Unraveling the RNA Binding Properties of the Iron-Sulfur Zinc Finger Protein CPSF30.

Identifieur interne : 000005 ( Main/Exploration ); précédent : 000004; suivant : 000006

Unraveling the RNA Binding Properties of the Iron-Sulfur Zinc Finger Protein CPSF30.

Auteurs : Jordan D. Pritts [États-Unis] ; Matthew S. Hursey [États-Unis] ; Jamie L. Michalek [États-Unis] ; Sharon Batelu [États-Unis] ; Timothy L. Stemmler [États-Unis] ; Sarah L J. Michel [États-Unis]

Source :

Biochemistry [ 1520-4995 ] ; 2020.

RBID : pubmed:32027124

Descripteurs français

English descriptors

KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Cattle (MeSH), Cleavage And Polyadenylation Specificity Factor (chemistry), Cleavage And Polyadenylation Specificity Factor (genetics), Cleavage And Polyadenylation Specificity Factor (metabolism), Cobalt (chemistry), Iron-Sulfur Proteins (chemistry), Iron-Sulfur Proteins (genetics), Iron-Sulfur Proteins (metabolism), Mutation (MeSH), Poly U (metabolism), Protein Binding (MeSH), RNA Precursors (genetics), RNA Precursors (metabolism), Zinc (chemistry), Zinc Fingers (MeSH), alpha-Synuclein (genetics).
MESH :
- chemical , chemistry : Cleavage And Polyadenylation Specificity Factor, Cobalt, Iron-Sulfur Proteins, Zinc.
- chemical , genetics : Cleavage And Polyadenylation Specificity Factor, Iron-Sulfur Proteins, RNA Precursors, alpha-Synuclein.
- chemical , metabolism : Cleavage And Polyadenylation Specificity Factor, Iron-Sulfur Proteins, Poly U, RNA Precursors.
- Amino Acid Sequence, Animals, Cattle, Mutation, Protein Binding, Zinc Fingers.

Abstract

Cleavage and polyadenylation specificity factor 30 (CPSF30) is a "zinc finger" protein that plays a crucial role in the transition of pre-mRNA to RNA. CPSF30 contains five conserved CCCH domains and a CCHC "zinc knuckle" domain. CPSF30 activity is critical for pre-mRNA processing. A truncated form of the protein, in which only the CCCH domains are present, has been shown to specifically bind AU-rich pre-mRNA targets; however, the RNA binding and recognition properties of full-length CPSF30 are not known. Herein, we report the isolation and biochemical characterization of full-length CPSF30. We report that CPSF30 contains one 2Fe-2S cluster in addition to five zinc ions, as measured by inductively coupled plasma mass spectrometry, ultraviolet-visible spectroscopy, and X-ray absorption spectroscopy. Utilizing fluorescence anisotropy RNA binding assays, we show that full-length CPSF30 has high binding affinity for two types of pre-mRNA targets, AAUAAA and polyU, both of which are conserved sequence motifs present in the majority of pre-mRNAs. Binding to the AAUAAA motif requires that the five CCCH domains of CPSF30 be present, whereas binding to polyU sequences requires the entire, full-length CPSF30. These findings implicate the CCHC "zinc knuckle" present in the full-length protein as being critical for mediating polyU binding. We also report that truncated forms of the protein, containing either just two CCCH domains (ZF2 and ZF3) or the CCHC "zinc knuckle" domain, do not exhibit any RNA binding, indicating that CPSF30/RNA binding requires several ZF (and/or Fe-S cluster) domains working in concert to mediate RNA recognition.

DOI: 10.1021/acs.biochem.9b01065
PubMed: 32027124

Affiliations:

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Le document en format XML

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<series><title level="j">Biochemistry</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term>
<term>Animals (MeSH)</term>
<term>Cattle (MeSH)</term>
<term>Cleavage And Polyadenylation Specificity Factor (chemistry)</term>
<term>Cleavage And Polyadenylation Specificity Factor (genetics)</term>
<term>Cleavage And Polyadenylation Specificity Factor (metabolism)</term>
<term>Cobalt (chemistry)</term>
<term>Iron-Sulfur Proteins (chemistry)</term>
<term>Iron-Sulfur Proteins (genetics)</term>
<term>Iron-Sulfur Proteins (metabolism)</term>
<term>Mutation (MeSH)</term>
<term>Poly U (metabolism)</term>
<term>Protein Binding (MeSH)</term>
<term>RNA Precursors (genetics)</term>
<term>RNA Precursors (metabolism)</term>
<term>Zinc (chemistry)</term>
<term>Zinc Fingers (MeSH)</term>
<term>alpha-Synuclein (genetics)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Bovins (MeSH)</term>
<term>Cobalt (composition chimique)</term>
<term>Doigts de zinc (MeSH)</term>
<term>Facteur de spécificité de clivage et polyadénylation (composition chimique)</term>
<term>Facteur de spécificité de clivage et polyadénylation (génétique)</term>
<term>Facteur de spécificité de clivage et polyadénylation (métabolisme)</term>
<term>Ferrosulfoprotéines (composition chimique)</term>
<term>Ferrosulfoprotéines (génétique)</term>
<term>Ferrosulfoprotéines (métabolisme)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Mutation (MeSH)</term>
<term>Poly U (métabolisme)</term>
<term>Précurseurs des ARN (génétique)</term>
<term>Précurseurs des ARN (métabolisme)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Zinc (composition chimique)</term>
<term>alpha-Synucléine (génétique)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Cleavage And Polyadenylation Specificity Factor</term>
<term>Cobalt</term>
<term>Iron-Sulfur Proteins</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Cleavage And Polyadenylation Specificity Factor</term>
<term>Iron-Sulfur Proteins</term>
<term>RNA Precursors</term>
<term>alpha-Synuclein</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Cleavage And Polyadenylation Specificity Factor</term>
<term>Iron-Sulfur Proteins</term>
<term>Poly U</term>
<term>RNA Precursors</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Cobalt</term>
<term>Facteur de spécificité de clivage et polyadénylation</term>
<term>Ferrosulfoprotéines</term>
<term>Zinc</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Facteur de spécificité de clivage et polyadénylation</term>
<term>Ferrosulfoprotéines</term>
<term>Précurseurs des ARN</term>
<term>alpha-Synucléine</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Facteur de spécificité de clivage et polyadénylation</term>
<term>Ferrosulfoprotéines</term>
<term>Poly U</term>
<term>Précurseurs des ARN</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cattle</term>
<term>Mutation</term>
<term>Protein Binding</term>
<term>Zinc Fingers</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Bovins</term>
<term>Doigts de zinc</term>
<term>Liaison aux protéines</term>
<term>Mutation</term>
<term>Séquence d'acides aminés</term>
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<front><div type="abstract" xml:lang="en">Cleavage and polyadenylation specificity factor 30 (CPSF30) is a "zinc finger" protein that plays a crucial role in the transition of pre-mRNA to RNA. CPSF30 contains five conserved CCCH domains and a CCHC "zinc knuckle" domain. CPSF30 activity is critical for pre-mRNA processing. A truncated form of the protein, in which only the CCCH domains are present, has been shown to specifically bind AU-rich pre-mRNA targets; however, the RNA binding and recognition properties of full-length CPSF30 are not known. Herein, we report the isolation and biochemical characterization of full-length CPSF30. We report that CPSF30 contains one 2Fe-2S cluster in addition to five zinc ions, as measured by inductively coupled plasma mass spectrometry, ultraviolet-visible spectroscopy, and X-ray absorption spectroscopy. Utilizing fluorescence anisotropy RNA binding assays, we show that full-length CPSF30 has high binding affinity for two types of pre-mRNA targets, AAUAAA and polyU, both of which are conserved sequence motifs present in the majority of pre-mRNAs. Binding to the AAUAAA motif requires that the five CCCH domains of CPSF30 be present, whereas binding to polyU sequences requires the entire, full-length CPSF30. These findings implicate the CCHC "zinc knuckle" present in the full-length protein as being critical for mediating polyU binding. We also report that truncated forms of the protein, containing either just two CCCH domains (ZF2 and ZF3) or the CCHC "zinc knuckle" domain, do not exhibit any RNA binding, indicating that CPSF30/RNA binding requires several ZF (and/or Fe-S cluster) domains working in concert to mediate RNA recognition.</div>
</front>
</TEI>
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<DateCompleted><Year>2020</Year>
<Month>10</Month>
<Day>16</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>10</Month>
<Day>16</Day>
</DateRevised>
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<JournalIssue CitedMedium="Internet"><Volume>59</Volume>
<Issue>8</Issue>
<PubDate><Year>2020</Year>
<Month>03</Month>
<Day>03</Day>
</PubDate>
</JournalIssue>
<Title>Biochemistry</Title>
<ISOAbbreviation>Biochemistry</ISOAbbreviation>
</Journal>
<ArticleTitle>Unraveling the RNA Binding Properties of the Iron-Sulfur Zinc Finger Protein CPSF30.</ArticleTitle>
<Pagination><MedlinePgn>970-982</MedlinePgn>
</Pagination>
<ELocationID EIdType="doi" ValidYN="Y">10.1021/acs.biochem.9b01065</ELocationID>
<Abstract><AbstractText>Cleavage and polyadenylation specificity factor 30 (CPSF30) is a "zinc finger" protein that plays a crucial role in the transition of pre-mRNA to RNA. CPSF30 contains five conserved CCCH domains and a CCHC "zinc knuckle" domain. CPSF30 activity is critical for pre-mRNA processing. A truncated form of the protein, in which only the CCCH domains are present, has been shown to specifically bind AU-rich pre-mRNA targets; however, the RNA binding and recognition properties of full-length CPSF30 are not known. Herein, we report the isolation and biochemical characterization of full-length CPSF30. We report that CPSF30 contains one 2Fe-2S cluster in addition to five zinc ions, as measured by inductively coupled plasma mass spectrometry, ultraviolet-visible spectroscopy, and X-ray absorption spectroscopy. Utilizing fluorescence anisotropy RNA binding assays, we show that full-length CPSF30 has high binding affinity for two types of pre-mRNA targets, AAUAAA and polyU, both of which are conserved sequence motifs present in the majority of pre-mRNAs. Binding to the AAUAAA motif requires that the five CCCH domains of CPSF30 be present, whereas binding to polyU sequences requires the entire, full-length CPSF30. These findings implicate the CCHC "zinc knuckle" present in the full-length protein as being critical for mediating polyU binding. We also report that truncated forms of the protein, containing either just two CCCH domains (ZF2 and ZF3) or the CCHC "zinc knuckle" domain, do not exhibit any RNA binding, indicating that CPSF30/RNA binding requires several ZF (and/or Fe-S cluster) domains working in concert to mediate RNA recognition.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Pritts</LastName>
<ForeName>Jordan D</ForeName>
<Initials>JD</Initials>
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<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201-1180, United States.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Hursey</LastName>
<ForeName>Matthew S</ForeName>
<Initials>MS</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201-1180, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Michalek</LastName>
<ForeName>Jamie L</ForeName>
<Initials>JL</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201-1180, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Batelu</LastName>
<ForeName>Sharon</ForeName>
<Initials>S</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences, Wayne State University, Detroit, Michigan 48201, United States.</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Stemmler</LastName>
<ForeName>Timothy L</ForeName>
<Initials>TL</Initials>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences, Wayne State University, Detroit, Michigan 48201, United States.</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Michel</LastName>
<ForeName>Sarah L J</ForeName>
<Initials>SLJ</Initials>
<Identifier Source="ORCID">0000-0002-6366-2453</Identifier>
<AffiliationInfo><Affiliation>Department of Pharmaceutical Sciences, School of Pharmacy, University of Maryland, Baltimore, Maryland 21201-1180, United States.</Affiliation>
</AffiliationInfo>
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<Language>eng</Language>
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<PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType>
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<ArticleDate DateType="Electronic"><Year>2020</Year>
<Month>02</Month>
<Day>19</Day>
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<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Biochemistry</MedlineTA>
<NlmUniqueID>0370623</NlmUniqueID>
<ISSNLinking>0006-2960</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D039223">Cleavage And Polyadenylation Specificity Factor</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D012322">RNA Precursors</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D051844">alpha-Synuclein</NameOfSubstance>
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<Chemical><RegistryNumber>27416-86-0</RegistryNumber>
<NameOfSubstance UI="D011072">Poly U</NameOfSubstance>
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<Chemical><RegistryNumber>3G0H8C9362</RegistryNumber>
<NameOfSubstance UI="D003035">Cobalt</NameOfSubstance>
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<Chemical><RegistryNumber>J41CSQ7QDS</RegistryNumber>
<NameOfSubstance UI="D015032">Zinc</NameOfSubstance>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D039223" MajorTopicYN="N">Cleavage And Polyadenylation Specificity Factor</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D003035" MajorTopicYN="N">Cobalt</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
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   |texte=   Unraveling the RNA Binding Properties of the Iron-Sulfur Zinc Finger Protein CPSF30.
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Unraveling the RNA Binding Properties of the Iron-Sulfur Zinc Finger Protein CPSF30.

Unraveling the RNA Binding Properties of the Iron-Sulfur Zinc Finger Protein CPSF30.

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