hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing
hLodestar/HuF2 belongs to the SNF2 family of proteins. This family of proteins has been shown to play a critical role in altering protein–DNA interactions in a variety of cellular contexts. We have identified an unexpected interaction between hLodestar/HuF2 and CDC5L in both the yeast two-hybrid sys...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2003-09, Vol.308 (4), p.793-801 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Leonard, Deana Ajuh, Paul Lamond, Angus I Legerski, Randy J |
| description | hLodestar/HuF2 belongs to the SNF2 family of proteins. This family of proteins has been shown to play a critical role in altering protein–DNA interactions in a variety of cellular contexts. We have identified an unexpected interaction between hLodestar/HuF2 and CDC5L in both the yeast two-hybrid system and HeLa nuclear extract. CDC5L is a well-characterized pre-mRNA splicing factor in yeast and humans. Our findings demonstrate that hLodestar/HuF2 associates with human splicing complexes. We also found that a truncated hLodestar/HuF2 polypeptide that overlaps with the CDC5L-binding region can inhibit pre-mRNA splicing by disrupting spliceosome assembly. These findings indicate that hLodestar/HuF2 may have a role in pre-mRNA splicing. These data are consistent with a close co-ordination of the transcription and splicing pathways in eukaryotes. Although many members of the DExH/D helicase superfamily have been linked to pre-mRNA splicing, this is the first SNF2 family member to be implicated in this pathway. |
| doi_str_mv | 10.1016/S0006-291X(03)01486-4 |
| format | Article |
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This family of proteins has been shown to play a critical role in altering protein–DNA interactions in a variety of cellular contexts. We have identified an unexpected interaction between hLodestar/HuF2 and CDC5L in both the yeast two-hybrid system and HeLa nuclear extract. CDC5L is a well-characterized pre-mRNA splicing factor in yeast and humans. Our findings demonstrate that hLodestar/HuF2 associates with human splicing complexes. We also found that a truncated hLodestar/HuF2 polypeptide that overlaps with the CDC5L-binding region can inhibit pre-mRNA splicing by disrupting spliceosome assembly. These findings indicate that hLodestar/HuF2 may have a role in pre-mRNA splicing. These data are consistent with a close co-ordination of the transcription and splicing pathways in eukaryotes. Although many members of the DExH/D helicase superfamily have been linked to pre-mRNA splicing, this is the first SNF2 family member to be implicated in this pathway.</description><identifier>ISSN: 0006-291X</identifier><identifier>EISSN: 1090-2104</identifier><identifier>DOI: 10.1016/S0006-291X(03)01486-4</identifier><identifier>PMID: 12927788</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Adenosine Triphosphatases ; Alternative Splicing ; Blotting, Western ; Carrier Proteins - chemistry ; Carrier Proteins - metabolism ; CDC5L ; Cell Cycle Proteins - chemistry ; Cell Cycle Proteins - metabolism ; Cell Nucleus - metabolism ; Cloning, Molecular ; DNA - metabolism ; DNA-Binding Proteins ; Drosophila Proteins ; Electrophoresis, Polyacrylamide Gel ; HeLa Cells ; hLodestar/HuF2 ; Humans ; Mass Spectrometry ; Models, Genetic ; Pre-mRNA splicing ; Precipitin Tests ; Protein Binding ; RNA Splicing ; RNA, Messenger - metabolism ; SNF2 ; Spliceosome ; Transcription Factors - chemistry ; Transcription Factors - metabolism ; Transcription Factors - physiology ; Transcription, Genetic ; Two-Hybrid System Techniques</subject><ispartof>Biochemical and biophysical research communications, 2003-09, Vol.308 (4), p.793-801</ispartof><rights>2003 Elsevier Inc.</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c392t-11c96a4d22d4f87f7e20ee39024e6ec4ce758030277d8163810d8b7108780ffe3</citedby><cites>FETCH-LOGICAL-c392t-11c96a4d22d4f87f7e20ee39024e6ec4ce758030277d8163810d8b7108780ffe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0006291X03014864$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,776,780,3537,27903,27904,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12927788$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Leonard, Deana</creatorcontrib><creatorcontrib>Ajuh, Paul</creatorcontrib><creatorcontrib>Lamond, Angus I</creatorcontrib><creatorcontrib>Legerski, Randy J</creatorcontrib><title>hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>hLodestar/HuF2 belongs to the SNF2 family of proteins. This family of proteins has been shown to play a critical role in altering protein–DNA interactions in a variety of cellular contexts. We have identified an unexpected interaction between hLodestar/HuF2 and CDC5L in both the yeast two-hybrid system and HeLa nuclear extract. CDC5L is a well-characterized pre-mRNA splicing factor in yeast and humans. Our findings demonstrate that hLodestar/HuF2 associates with human splicing complexes. We also found that a truncated hLodestar/HuF2 polypeptide that overlaps with the CDC5L-binding region can inhibit pre-mRNA splicing by disrupting spliceosome assembly. These findings indicate that hLodestar/HuF2 may have a role in pre-mRNA splicing. These data are consistent with a close co-ordination of the transcription and splicing pathways in eukaryotes. Although many members of the DExH/D helicase superfamily have been linked to pre-mRNA splicing, this is the first SNF2 family member to be implicated in this pathway.</description><subject>Adenosine Triphosphatases</subject><subject>Alternative Splicing</subject><subject>Blotting, Western</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - metabolism</subject><subject>CDC5L</subject><subject>Cell Cycle Proteins - chemistry</subject><subject>Cell Cycle Proteins - metabolism</subject><subject>Cell Nucleus - metabolism</subject><subject>Cloning, Molecular</subject><subject>DNA - metabolism</subject><subject>DNA-Binding Proteins</subject><subject>Drosophila Proteins</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>HeLa Cells</subject><subject>hLodestar/HuF2</subject><subject>Humans</subject><subject>Mass Spectrometry</subject><subject>Models, Genetic</subject><subject>Pre-mRNA splicing</subject><subject>Precipitin Tests</subject><subject>Protein Binding</subject><subject>RNA Splicing</subject><subject>RNA, Messenger - metabolism</subject><subject>SNF2</subject><subject>Spliceosome</subject><subject>Transcription Factors - chemistry</subject><subject>Transcription Factors - metabolism</subject><subject>Transcription Factors - physiology</subject><subject>Transcription, Genetic</subject><subject>Two-Hybrid System Techniques</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1rGzEQhkVpaZyPn9Cyp9IcNp6R5JV0CsaN64BJIGkhN7GWZhuF9a4jrV3y77P-oD36NAPzzMzLw9gXhCsELIaPAFDk3ODTdxCXgFIXufzABggGco4gP7LBP-SEnab0AoAoC_OZnSA3XCmtB2z2PG89pa6Mw9l6yrPQdBRL16Xsb-ies8mPyWielY3PQupnm7beUN832SpSvny4G2dpVQcXmj_n7FNV1okuDvWM_Z7e_JrM8vn9z9vJeJ47YXiXIzpTlNJz7mWlVaWIA5EwwCUV5KQjNdIgoI_nNRZCI3i9UAhaaagqEmfs2_7uKrav6z65XYbkqK7Lhtp1skqMlDBCHQVRa6GV2YKjPehim1Kkyq5iWJbxzSLYrWu7c223Ii0Iu3NtZb_39fBgvViS_791kNsD13uAeh-bQNEmF6hx5EMk11nfhiMv3gFxcovv</recordid><startdate>20030905</startdate><enddate>20030905</enddate><creator>Leonard, Deana</creator><creator>Ajuh, Paul</creator><creator>Lamond, Angus I</creator><creator>Legerski, Randy J</creator><general>Elsevier Inc</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>20030905</creationdate><title>hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing</title><author>Leonard, Deana ; Ajuh, Paul ; Lamond, Angus I ; Legerski, Randy J</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c392t-11c96a4d22d4f87f7e20ee39024e6ec4ce758030277d8163810d8b7108780ffe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Adenosine Triphosphatases</topic><topic>Alternative Splicing</topic><topic>Blotting, Western</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - metabolism</topic><topic>CDC5L</topic><topic>Cell Cycle Proteins - chemistry</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cell Nucleus - metabolism</topic><topic>Cloning, Molecular</topic><topic>DNA - metabolism</topic><topic>DNA-Binding Proteins</topic><topic>Drosophila Proteins</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>HeLa Cells</topic><topic>hLodestar/HuF2</topic><topic>Humans</topic><topic>Mass Spectrometry</topic><topic>Models, Genetic</topic><topic>Pre-mRNA splicing</topic><topic>Precipitin Tests</topic><topic>Protein Binding</topic><topic>RNA Splicing</topic><topic>RNA, Messenger - metabolism</topic><topic>SNF2</topic><topic>Spliceosome</topic><topic>Transcription Factors - chemistry</topic><topic>Transcription Factors - metabolism</topic><topic>Transcription Factors - physiology</topic><topic>Transcription, Genetic</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Leonard, Deana</creatorcontrib><creatorcontrib>Ajuh, Paul</creatorcontrib><creatorcontrib>Lamond, Angus I</creatorcontrib><creatorcontrib>Legerski, Randy J</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Leonard, Deana</au><au>Ajuh, Paul</au><au>Lamond, Angus I</au><au>Legerski, Randy J</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2003-09-05</date><risdate>2003</risdate><volume>308</volume><issue>4</issue><spage>793</spage><epage>801</epage><pages>793-801</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><abstract>hLodestar/HuF2 belongs to the SNF2 family of proteins. This family of proteins has been shown to play a critical role in altering protein–DNA interactions in a variety of cellular contexts. We have identified an unexpected interaction between hLodestar/HuF2 and CDC5L in both the yeast two-hybrid system and HeLa nuclear extract. CDC5L is a well-characterized pre-mRNA splicing factor in yeast and humans. Our findings demonstrate that hLodestar/HuF2 associates with human splicing complexes. We also found that a truncated hLodestar/HuF2 polypeptide that overlaps with the CDC5L-binding region can inhibit pre-mRNA splicing by disrupting spliceosome assembly. These findings indicate that hLodestar/HuF2 may have a role in pre-mRNA splicing. These data are consistent with a close co-ordination of the transcription and splicing pathways in eukaryotes. Although many members of the DExH/D helicase superfamily have been linked to pre-mRNA splicing, this is the first SNF2 family member to be implicated in this pathway.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>12927788</pmid><doi>10.1016/S0006-291X(03)01486-4</doi><tpages>9</tpages></addata></record> |
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| subjects | Adenosine Triphosphatases Alternative Splicing Blotting, Western Carrier Proteins - chemistry Carrier Proteins - metabolism CDC5L Cell Cycle Proteins - chemistry Cell Cycle Proteins - metabolism Cell Nucleus - metabolism Cloning, Molecular DNA - metabolism DNA-Binding Proteins Drosophila Proteins Electrophoresis, Polyacrylamide Gel HeLa Cells hLodestar/HuF2 Humans Mass Spectrometry Models, Genetic Pre-mRNA splicing Precipitin Tests Protein Binding RNA Splicing RNA, Messenger - metabolism SNF2 Spliceosome Transcription Factors - chemistry Transcription Factors - metabolism Transcription Factors - physiology Transcription, Genetic Two-Hybrid System Techniques |
| title | hLodestar/HuF2 interacts with CDC5L and is involved in pre-mRNA splicing |
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