retinoblastoma-binding protein related to a negative regulator of Ras in yeast

The growth suppression function of the retinoblastoma protein (Rb) is thought to be mediated by Rb binding to cellular proteins p48 is one of the major proteins that binds to a putative functional domain at the carboxy terminus of the Rb protein. Here we report the isolation of a full-length complem...

Ausführliche Beschreibung

Gespeichert in:
Bibliographische Detailangaben
Veröffentlicht in:Nature (London) 1993-08, Vol.364 (6438), p.648-652
Hauptverfasser: Qian, Y.W, Wang, Y.C.J, Hollingsworth, R.E. Jr, Jones, D, Ling, N, Lee, E.Y.H.P
Format: Artikel
Sprache:eng
Schlagworte:
Online-Zugang:Volltext
Tags: Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
container_end_page 652
container_issue 6438
container_start_page 648
container_title Nature (London)
container_volume 364
creator Qian, Y.W
Wang, Y.C.J
Hollingsworth, R.E. Jr
Jones, D
Ling, N
Lee, E.Y.H.P
description The growth suppression function of the retinoblastoma protein (Rb) is thought to be mediated by Rb binding to cellular proteins p48 is one of the major proteins that binds to a putative functional domain at the carboxy terminus of the Rb protein. Here we report the isolation of a full-length complementary DNA (RbAp4g) encoding p48. Complex formation between p48 and Rb occurs in vitro and in vivo, and apparently involves direct interaction between the proteins. Like Rb, p48 is a ubiquitously expressed nuclear protein. RbAp4g share sequence homology with MSI1, a negative regulator of the Ras-cyclic AMP pathway in the yeast Saccharomyces cerevisiae. Furthermore, like MSI1, human RbAp48 suppresses the heat-shock sensitivity of the yeast ira1 strains and RAS2(Val19) strains. Interaction with p48 may be one of the mechanisms for suppression of growth mediated by Rb.
doi_str_mv 10.1038/364648a0
format Article
fullrecord <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_75866459</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>75866459</sourcerecordid><originalsourceid>FETCH-LOGICAL-c489t-8e7cd1bd9fe85a33148ba7dc8e10ef56470b754be4507097e21d32dbaa83886a3</originalsourceid><addsrcrecordid>eNqF0V1r1UAQBuBFLPW0Cv4BMYhIexGdzX5NLqVULRQFtddhkkxCSs5u3U2E_nv3cI4VRPBqYebh3dkdIZ5LeCtB4TtltdVI8EhspHa21BbdY7EBqLAEVPaJOEnpFgCMdPpYHKMyUFd6Iz5HXiYf2pnSErZUtpPvJz8WdzEsPPki8kwL98USCio8j7RMPzlXxzXXQyzCUHylVGR5zzniqTgaaE787HCeipsPl98vPpXXXz5eXby_LjuN9VIiu66XbV8PjIaUkhpbcn2HLIEHY7WD1hndsjbgoHZcyV5VfUuECtGSOhVv9rl5zh8rp6XZTqnjeSbPYU2NM2itNvV_obRW1ogyw1d_wduwRp8f0VSg9U7pjM72qIshpchDcxenLcX7RkKzW0TzexGZvjjkre2W-wd4-Pncf33oU-poHiL5bkoPTKNxtdux8z1LueNHjn_G-seVL_d2oNDQGHPczbcKpIL8v4DSqF_iDaS5</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>204461984</pqid></control><display><type>article</type><title>retinoblastoma-binding protein related to a negative regulator of Ras in yeast</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><source>Nature Journals Online</source><creator>Qian, Y.W ; Wang, Y.C.J ; Hollingsworth, R.E. Jr ; Jones, D ; Ling, N ; Lee, E.Y.H.P</creator><creatorcontrib>Qian, Y.W ; Wang, Y.C.J ; Hollingsworth, R.E. Jr ; Jones, D ; Ling, N ; Lee, E.Y.H.P</creatorcontrib><description>The growth suppression function of the retinoblastoma protein (Rb) is thought to be mediated by Rb binding to cellular proteins p48 is one of the major proteins that binds to a putative functional domain at the carboxy terminus of the Rb protein. Here we report the isolation of a full-length complementary DNA (RbAp4g) encoding p48. Complex formation between p48 and Rb occurs in vitro and in vivo, and apparently involves direct interaction between the proteins. Like Rb, p48 is a ubiquitously expressed nuclear protein. RbAp4g share sequence homology with MSI1, a negative regulator of the Ras-cyclic AMP pathway in the yeast Saccharomyces cerevisiae. Furthermore, like MSI1, human RbAp48 suppresses the heat-shock sensitivity of the yeast ira1 strains and RAS2(Val19) strains. Interaction with p48 may be one of the mechanisms for suppression of growth mediated by Rb.</description><identifier>ISSN: 0028-0836</identifier><identifier>EISSN: 1476-4687</identifier><identifier>DOI: 10.1038/364648a0</identifier><identifier>PMID: 8350924</identifier><identifier>CODEN: NATUAS</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>Amino Acid Sequence ; amino acid sequences ; Base Sequence ; binding proteins ; Biological and medical sciences ; Biotechnology ; Carrier Proteins - chemistry ; Carrier Proteins - genetics ; Carrier Proteins - metabolism ; cDNA ; Cell cycle, cell proliferation ; Cell physiology ; Cellular biology ; Chromatin Assembly Factor-1 ; cloning ; complex ; DNA ; DNA-Binding Proteins ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - chemistry ; genes ; Hot Temperature ; Humanities and Social Sciences ; Humans ; letter ; man ; Molecular and cellular biology ; Molecular Sequence Data ; multidisciplinary ; Nuclear Proteins - chemistry ; Nuclear Proteins - genetics ; Nuclear Proteins - metabolism ; nucleotide sequence ; nucleotide sequences ; predictions ; Protein Binding ; protein p48 ; Proteins ; RbAp48 gene ; Recombinant Proteins - metabolism ; Retinoblastoma Protein - metabolism ; retinoblastoma-binding protein ; Retinoblastoma-Binding Protein 4 ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae - physiology ; Saccharomyces cerevisiae Proteins ; Science ; Science (multidisciplinary) ; Sequence Homology, Amino Acid ; Tumor Cells, Cultured ; tumor suppressor genes ; Yeast ; Yeasts</subject><ispartof>Nature (London), 1993-08, Vol.364 (6438), p.648-652</ispartof><rights>Springer Nature Limited 1993</rights><rights>1993 INIST-CNRS</rights><rights>Copyright Macmillan Journals Ltd. Aug 12, 1993</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c489t-8e7cd1bd9fe85a33148ba7dc8e10ef56470b754be4507097e21d32dbaa83886a3</citedby><cites>FETCH-LOGICAL-c489t-8e7cd1bd9fe85a33148ba7dc8e10ef56470b754be4507097e21d32dbaa83886a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1038/364648a0$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1038/364648a0$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=4857974$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8350924$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Qian, Y.W</creatorcontrib><creatorcontrib>Wang, Y.C.J</creatorcontrib><creatorcontrib>Hollingsworth, R.E. Jr</creatorcontrib><creatorcontrib>Jones, D</creatorcontrib><creatorcontrib>Ling, N</creatorcontrib><creatorcontrib>Lee, E.Y.H.P</creatorcontrib><title>retinoblastoma-binding protein related to a negative regulator of Ras in yeast</title><title>Nature (London)</title><addtitle>Nature</addtitle><addtitle>Nature</addtitle><description>The growth suppression function of the retinoblastoma protein (Rb) is thought to be mediated by Rb binding to cellular proteins p48 is one of the major proteins that binds to a putative functional domain at the carboxy terminus of the Rb protein. Here we report the isolation of a full-length complementary DNA (RbAp4g) encoding p48. Complex formation between p48 and Rb occurs in vitro and in vivo, and apparently involves direct interaction between the proteins. Like Rb, p48 is a ubiquitously expressed nuclear protein. RbAp4g share sequence homology with MSI1, a negative regulator of the Ras-cyclic AMP pathway in the yeast Saccharomyces cerevisiae. Furthermore, like MSI1, human RbAp48 suppresses the heat-shock sensitivity of the yeast ira1 strains and RAS2(Val19) strains. Interaction with p48 may be one of the mechanisms for suppression of growth mediated by Rb.</description><subject>Amino Acid Sequence</subject><subject>amino acid sequences</subject><subject>Base Sequence</subject><subject>binding proteins</subject><subject>Biological and medical sciences</subject><subject>Biotechnology</subject><subject>Carrier Proteins - chemistry</subject><subject>Carrier Proteins - genetics</subject><subject>Carrier Proteins - metabolism</subject><subject>cDNA</subject><subject>Cell cycle, cell proliferation</subject><subject>Cell physiology</subject><subject>Cellular biology</subject><subject>Chromatin Assembly Factor-1</subject><subject>cloning</subject><subject>complex</subject><subject>DNA</subject><subject>DNA-Binding Proteins</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - chemistry</subject><subject>genes</subject><subject>Hot Temperature</subject><subject>Humanities and Social Sciences</subject><subject>Humans</subject><subject>letter</subject><subject>man</subject><subject>Molecular and cellular biology</subject><subject>Molecular Sequence Data</subject><subject>multidisciplinary</subject><subject>Nuclear Proteins - chemistry</subject><subject>Nuclear Proteins - genetics</subject><subject>Nuclear Proteins - metabolism</subject><subject>nucleotide sequence</subject><subject>nucleotide sequences</subject><subject>predictions</subject><subject>Protein Binding</subject><subject>protein p48</subject><subject>Proteins</subject><subject>RbAp48 gene</subject><subject>Recombinant Proteins - metabolism</subject><subject>Retinoblastoma Protein - metabolism</subject><subject>retinoblastoma-binding protein</subject><subject>Retinoblastoma-Binding Protein 4</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Saccharomyces cerevisiae Proteins</subject><subject>Science</subject><subject>Science (multidisciplinary)</subject><subject>Sequence Homology, Amino Acid</subject><subject>Tumor Cells, Cultured</subject><subject>tumor suppressor genes</subject><subject>Yeast</subject><subject>Yeasts</subject><issn>0028-0836</issn><issn>1476-4687</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>8G5</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><sourceid>GUQSH</sourceid><sourceid>M2O</sourceid><recordid>eNqF0V1r1UAQBuBFLPW0Cv4BMYhIexGdzX5NLqVULRQFtddhkkxCSs5u3U2E_nv3cI4VRPBqYebh3dkdIZ5LeCtB4TtltdVI8EhspHa21BbdY7EBqLAEVPaJOEnpFgCMdPpYHKMyUFd6Iz5HXiYf2pnSErZUtpPvJz8WdzEsPPki8kwL98USCio8j7RMPzlXxzXXQyzCUHylVGR5zzniqTgaaE787HCeipsPl98vPpXXXz5eXby_LjuN9VIiu66XbV8PjIaUkhpbcn2HLIEHY7WD1hndsjbgoHZcyV5VfUuECtGSOhVv9rl5zh8rp6XZTqnjeSbPYU2NM2itNvV_obRW1ogyw1d_wduwRp8f0VSg9U7pjM72qIshpchDcxenLcX7RkKzW0TzexGZvjjkre2W-wd4-Pncf33oU-poHiL5bkoPTKNxtdux8z1LueNHjn_G-seVL_d2oNDQGHPczbcKpIL8v4DSqF_iDaS5</recordid><startdate>19930812</startdate><enddate>19930812</enddate><creator>Qian, Y.W</creator><creator>Wang, Y.C.J</creator><creator>Hollingsworth, R.E. Jr</creator><creator>Jones, D</creator><creator>Ling, N</creator><creator>Lee, E.Y.H.P</creator><general>Nature Publishing Group UK</general><general>Nature Publishing</general><general>Nature Publishing Group</general><scope>FBQ</scope><scope>IQODW</scope><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>3V.</scope><scope>7QG</scope><scope>7QL</scope><scope>7QP</scope><scope>7QR</scope><scope>7RV</scope><scope>7SN</scope><scope>7SS</scope><scope>7ST</scope><scope>7T5</scope><scope>7TG</scope><scope>7TK</scope><scope>7TM</scope><scope>7TO</scope><scope>7U9</scope><scope>7X2</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88G</scope><scope>88I</scope><scope>8AF</scope><scope>8AO</scope><scope>8C1</scope><scope>8FD</scope><scope>8FE</scope><scope>8FG</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>8G5</scope><scope>ABJCF</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>ARAPS</scope><scope>ATCPS</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BEC</scope><scope>BENPR</scope><scope>BGLVJ</scope><scope>BHPHI</scope><scope>BKSAR</scope><scope>C1K</scope><scope>CCPQU</scope><scope>D1I</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>GUQSH</scope><scope>H94</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>KB.</scope><scope>KB0</scope><scope>KL.</scope><scope>L6V</scope><scope>LK8</scope><scope>M0K</scope><scope>M0S</scope><scope>M1P</scope><scope>M2M</scope><scope>M2O</scope><scope>M2P</scope><scope>M7N</scope><scope>M7P</scope><scope>M7S</scope><scope>MBDVC</scope><scope>NAPCQ</scope><scope>P5Z</scope><scope>P62</scope><scope>P64</scope><scope>PATMY</scope><scope>PCBAR</scope><scope>PDBOC</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PSYQQ</scope><scope>PTHSS</scope><scope>PYCSY</scope><scope>Q9U</scope><scope>R05</scope><scope>RC3</scope><scope>S0X</scope><scope>SOI</scope><scope>7T3</scope><scope>7X8</scope></search><sort><creationdate>19930812</creationdate><title>retinoblastoma-binding protein related to a negative regulator of Ras in yeast</title><author>Qian, Y.W ; Wang, Y.C.J ; Hollingsworth, R.E. Jr ; Jones, D ; Ling, N ; Lee, E.Y.H.P</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c489t-8e7cd1bd9fe85a33148ba7dc8e10ef56470b754be4507097e21d32dbaa83886a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Amino Acid Sequence</topic><topic>amino acid sequences</topic><topic>Base Sequence</topic><topic>binding proteins</topic><topic>Biological and medical sciences</topic><topic>Biotechnology</topic><topic>Carrier Proteins - chemistry</topic><topic>Carrier Proteins - genetics</topic><topic>Carrier Proteins - metabolism</topic><topic>cDNA</topic><topic>Cell cycle, cell proliferation</topic><topic>Cell physiology</topic><topic>Cellular biology</topic><topic>Chromatin Assembly Factor-1</topic><topic>cloning</topic><topic>complex</topic><topic>DNA</topic><topic>DNA-Binding Proteins</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - chemistry</topic><topic>genes</topic><topic>Hot Temperature</topic><topic>Humanities and Social Sciences</topic><topic>Humans</topic><topic>letter</topic><topic>man</topic><topic>Molecular and cellular biology</topic><topic>Molecular Sequence Data</topic><topic>multidisciplinary</topic><topic>Nuclear Proteins - chemistry</topic><topic>Nuclear Proteins - genetics</topic><topic>Nuclear Proteins - metabolism</topic><topic>nucleotide sequence</topic><topic>nucleotide sequences</topic><topic>predictions</topic><topic>Protein Binding</topic><topic>protein p48</topic><topic>Proteins</topic><topic>RbAp48 gene</topic><topic>Recombinant Proteins - metabolism</topic><topic>Retinoblastoma Protein - metabolism</topic><topic>retinoblastoma-binding protein</topic><topic>Retinoblastoma-Binding Protein 4</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Saccharomyces cerevisiae Proteins</topic><topic>Science</topic><topic>Science (multidisciplinary)</topic><topic>Sequence Homology, Amino Acid</topic><topic>Tumor Cells, Cultured</topic><topic>tumor suppressor genes</topic><topic>Yeast</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Qian, Y.W</creatorcontrib><creatorcontrib>Wang, Y.C.J</creatorcontrib><creatorcontrib>Hollingsworth, R.E. Jr</creatorcontrib><creatorcontrib>Jones, D</creatorcontrib><creatorcontrib>Ling, N</creatorcontrib><creatorcontrib>Lee, E.Y.H.P</creatorcontrib><collection>AGRIS</collection><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Animal Behavior Abstracts</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Calcium &amp; Calcified Tissue Abstracts</collection><collection>Chemoreception Abstracts</collection><collection>Nursing &amp; Allied Health Database</collection><collection>Ecology Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Environment Abstracts</collection><collection>Immunology Abstracts</collection><collection>Meteorological &amp; Geoastrophysical Abstracts</collection><collection>Neurosciences Abstracts</collection><collection>Nucleic Acids Abstracts</collection><collection>Oncogenes and Growth Factors Abstracts</collection><collection>Virology and AIDS Abstracts</collection><collection>Agricultural Science Collection</collection><collection>Health &amp; Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Psychology Database (Alumni)</collection><collection>Science Database (Alumni Edition)</collection><collection>STEM Database</collection><collection>ProQuest Pharma Collection</collection><collection>Public Health Database</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Technology Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>Research Library (Alumni Edition)</collection><collection>Materials Science &amp; Engineering Collection</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>Advanced Technologies &amp; Aerospace Collection</collection><collection>Agricultural &amp; Environmental Science Collection</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>eLibrary</collection><collection>ProQuest Central</collection><collection>Technology Collection</collection><collection>Natural Science Collection</collection><collection>Earth, Atmospheric &amp; Aquatic Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Materials Science Collection</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>Research Library Prep</collection><collection>AIDS and Cancer Research Abstracts</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health &amp; Medical Complete (Alumni)</collection><collection>Materials Science Database</collection><collection>Nursing &amp; Allied Health Database (Alumni Edition)</collection><collection>Meteorological &amp; Geoastrophysical Abstracts - Academic</collection><collection>ProQuest Engineering Collection</collection><collection>ProQuest Biological Science Collection</collection><collection>Agricultural Science Database</collection><collection>Health &amp; Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Psychology Database</collection><collection>Research Library</collection><collection>Science Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biological Science Database</collection><collection>Engineering Database</collection><collection>Research Library (Corporate)</collection><collection>Nursing &amp; Allied Health Premium</collection><collection>Advanced Technologies &amp; Aerospace Database</collection><collection>ProQuest Advanced Technologies &amp; Aerospace Collection</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Environmental Science Database</collection><collection>Earth, Atmospheric &amp; Aquatic Science Database</collection><collection>Materials Science Collection</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest One Psychology</collection><collection>Engineering Collection</collection><collection>Environmental Science Collection</collection><collection>ProQuest Central Basic</collection><collection>University of Michigan</collection><collection>Genetics Abstracts</collection><collection>SIRS Editorial</collection><collection>Environment Abstracts</collection><collection>Human Genome Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Nature (London)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Qian, Y.W</au><au>Wang, Y.C.J</au><au>Hollingsworth, R.E. Jr</au><au>Jones, D</au><au>Ling, N</au><au>Lee, E.Y.H.P</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>retinoblastoma-binding protein related to a negative regulator of Ras in yeast</atitle><jtitle>Nature (London)</jtitle><stitle>Nature</stitle><addtitle>Nature</addtitle><date>1993-08-12</date><risdate>1993</risdate><volume>364</volume><issue>6438</issue><spage>648</spage><epage>652</epage><pages>648-652</pages><issn>0028-0836</issn><eissn>1476-4687</eissn><coden>NATUAS</coden><abstract>The growth suppression function of the retinoblastoma protein (Rb) is thought to be mediated by Rb binding to cellular proteins p48 is one of the major proteins that binds to a putative functional domain at the carboxy terminus of the Rb protein. Here we report the isolation of a full-length complementary DNA (RbAp4g) encoding p48. Complex formation between p48 and Rb occurs in vitro and in vivo, and apparently involves direct interaction between the proteins. Like Rb, p48 is a ubiquitously expressed nuclear protein. RbAp4g share sequence homology with MSI1, a negative regulator of the Ras-cyclic AMP pathway in the yeast Saccharomyces cerevisiae. Furthermore, like MSI1, human RbAp48 suppresses the heat-shock sensitivity of the yeast ira1 strains and RAS2(Val19) strains. Interaction with p48 may be one of the mechanisms for suppression of growth mediated by Rb.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>8350924</pmid><doi>10.1038/364648a0</doi><tpages>5</tpages></addata></record>
fulltext fulltext
identifier ISSN: 0028-0836
ispartof Nature (London), 1993-08, Vol.364 (6438), p.648-652
issn 0028-0836
1476-4687
language eng
recordid cdi_proquest_miscellaneous_75866459
source MEDLINE; Springer Nature - Complete Springer Journals; Nature Journals Online
subjects Amino Acid Sequence
amino acid sequences
Base Sequence
binding proteins
Biological and medical sciences
Biotechnology
Carrier Proteins - chemistry
Carrier Proteins - genetics
Carrier Proteins - metabolism
cDNA
Cell cycle, cell proliferation
Cell physiology
Cellular biology
Chromatin Assembly Factor-1
cloning
complex
DNA
DNA-Binding Proteins
Fundamental and applied biological sciences. Psychology
Fungal Proteins - chemistry
genes
Hot Temperature
Humanities and Social Sciences
Humans
letter
man
Molecular and cellular biology
Molecular Sequence Data
multidisciplinary
Nuclear Proteins - chemistry
Nuclear Proteins - genetics
Nuclear Proteins - metabolism
nucleotide sequence
nucleotide sequences
predictions
Protein Binding
protein p48
Proteins
RbAp48 gene
Recombinant Proteins - metabolism
Retinoblastoma Protein - metabolism
retinoblastoma-binding protein
Retinoblastoma-Binding Protein 4
Saccharomyces cerevisiae
Saccharomyces cerevisiae - physiology
Saccharomyces cerevisiae Proteins
Science
Science (multidisciplinary)
Sequence Homology, Amino Acid
Tumor Cells, Cultured
tumor suppressor genes
Yeast
Yeasts
title retinoblastoma-binding protein related to a negative regulator of Ras in yeast
url https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-19T20%3A12%3A11IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=retinoblastoma-binding%20protein%20related%20to%20a%20negative%20regulator%20of%20Ras%20in%20yeast&rft.jtitle=Nature%20(London)&rft.au=Qian,%20Y.W&rft.date=1993-08-12&rft.volume=364&rft.issue=6438&rft.spage=648&rft.epage=652&rft.pages=648-652&rft.issn=0028-0836&rft.eissn=1476-4687&rft.coden=NATUAS&rft_id=info:doi/10.1038/364648a0&rft_dat=%3Cproquest_cross%3E75866459%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=204461984&rft_id=info:pmid/8350924&rfr_iscdi=true