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Nep98p Is a Component of the Yeast Spindle Pole Body and Essential for Nuclear Division and Fusion
During the mating of yeast Saccharomyces cerevisiae , two haploid nuclei fuse to produce a diploid nucleus. This process requires the functions of BiP/Kar2p, a member of the Hsp70 family in the endoplasmic reticulum, and its partner protein, Jem1p. To investigate further the role of BiP and Jem1p in...
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| Published in: | The Journal of biological chemistry 2003-03, Vol.278 (11), p.9938-9943 |
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| Main Authors: | , , , , , |
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| cited_by | cdi_FETCH-LOGICAL-c456t-fefcebe891538df85add1157c42a8d605fbfba887662cee432dd6eb0b50179e3 |
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| container_end_page | 9943 |
| container_issue | 11 |
| container_start_page | 9938 |
| container_title | The Journal of biological chemistry |
| container_volume | 278 |
| creator | Nishikawa, Shuh-Ichi Terazawa, Yumiko Nakayama, Takeshi Hirata, Aiko Makio, Tadashi Endo, Toshiya |
| description | During the mating of yeast Saccharomyces cerevisiae , two haploid nuclei fuse to produce a diploid nucleus. This process requires the functions of BiP/Kar2p, a member of the
Hsp70 family in the endoplasmic reticulum, and its partner protein, Jem1p. To investigate further the role of BiP and Jem1p
in nuclear fusion, we screened for partner proteins for Jem1p by the yeast two-hybrid system and identified Nep98p. Nep98p
is an essential integral membrane protein of the nuclear envelope and is enriched in the spindle pole body (SPB), the sole
microtubule-organizing center in yeast. Temperature-sensitive nep98 mutant cells contain abnormal SPBs lacking the half-bridge, suggesting the essential role of Nep98p in the organization of
the normal SPB. Additionally, nep98 mutant cells show defects in mitotic nuclear division and nuclear fusion during mating. Because Jem1p is not required for
nuclear division, Nep98p probably has dual functions in Jem1p-dependent karyogamy and in Jem1p-independent nuclear division. |
| doi_str_mv | 10.1074/jbc.M210934200 |
| format | article |
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Hsp70 family in the endoplasmic reticulum, and its partner protein, Jem1p. To investigate further the role of BiP and Jem1p
in nuclear fusion, we screened for partner proteins for Jem1p by the yeast two-hybrid system and identified Nep98p. Nep98p
is an essential integral membrane protein of the nuclear envelope and is enriched in the spindle pole body (SPB), the sole
microtubule-organizing center in yeast. Temperature-sensitive nep98 mutant cells contain abnormal SPBs lacking the half-bridge, suggesting the essential role of Nep98p in the organization of
the normal SPB. Additionally, nep98 mutant cells show defects in mitotic nuclear division and nuclear fusion during mating. Because Jem1p is not required for
nuclear division, Nep98p probably has dual functions in Jem1p-dependent karyogamy and in Jem1p-independent nuclear division.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M210934200</identifier><identifier>PMID: 12493774</identifier><language>eng</language><publisher>United States: American Society for Biochemistry and Molecular Biology</publisher><subject>Amino Acid Sequence ; Cell Nucleus - metabolism ; G2 Phase ; Genes, Fungal ; HSP70 Heat-Shock Proteins - metabolism ; Membrane Proteins - chemistry ; Membrane Proteins - metabolism ; Membrane Proteins - physiology ; Microscopy, Electron ; Microscopy, Fluorescence ; Mitosis ; Molecular Chaperones ; Molecular Sequence Data ; Mutagenesis, Site-Directed ; Mutation ; Nuclear Proteins ; Plasmids - metabolism ; Protein Binding ; Protein Structure, Tertiary ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Saccharomyces cerevisiae Proteins - physiology ; Spindle Apparatus ; Temperature ; Two-Hybrid System Techniques</subject><ispartof>The Journal of biological chemistry, 2003-03, Vol.278 (11), p.9938-9943</ispartof><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c456t-fefcebe891538df85add1157c42a8d605fbfba887662cee432dd6eb0b50179e3</citedby><cites>FETCH-LOGICAL-c456t-fefcebe891538df85add1157c42a8d605fbfba887662cee432dd6eb0b50179e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/12493774$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Nishikawa, Shuh-Ichi</creatorcontrib><creatorcontrib>Terazawa, Yumiko</creatorcontrib><creatorcontrib>Nakayama, Takeshi</creatorcontrib><creatorcontrib>Hirata, Aiko</creatorcontrib><creatorcontrib>Makio, Tadashi</creatorcontrib><creatorcontrib>Endo, Toshiya</creatorcontrib><title>Nep98p Is a Component of the Yeast Spindle Pole Body and Essential for Nuclear Division and Fusion</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>During the mating of yeast Saccharomyces cerevisiae , two haploid nuclei fuse to produce a diploid nucleus. This process requires the functions of BiP/Kar2p, a member of the
Hsp70 family in the endoplasmic reticulum, and its partner protein, Jem1p. To investigate further the role of BiP and Jem1p
in nuclear fusion, we screened for partner proteins for Jem1p by the yeast two-hybrid system and identified Nep98p. Nep98p
is an essential integral membrane protein of the nuclear envelope and is enriched in the spindle pole body (SPB), the sole
microtubule-organizing center in yeast. Temperature-sensitive nep98 mutant cells contain abnormal SPBs lacking the half-bridge, suggesting the essential role of Nep98p in the organization of
the normal SPB. Additionally, nep98 mutant cells show defects in mitotic nuclear division and nuclear fusion during mating. Because Jem1p is not required for
nuclear division, Nep98p probably has dual functions in Jem1p-dependent karyogamy and in Jem1p-independent nuclear division.</description><subject>Amino Acid Sequence</subject><subject>Cell Nucleus - metabolism</subject><subject>G2 Phase</subject><subject>Genes, Fungal</subject><subject>HSP70 Heat-Shock Proteins - metabolism</subject><subject>Membrane Proteins - chemistry</subject><subject>Membrane Proteins - metabolism</subject><subject>Membrane Proteins - physiology</subject><subject>Microscopy, Electron</subject><subject>Microscopy, Fluorescence</subject><subject>Mitosis</subject><subject>Molecular Chaperones</subject><subject>Molecular Sequence Data</subject><subject>Mutagenesis, Site-Directed</subject><subject>Mutation</subject><subject>Nuclear Proteins</subject><subject>Plasmids - metabolism</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Saccharomyces cerevisiae Proteins - physiology</subject><subject>Spindle Apparatus</subject><subject>Temperature</subject><subject>Two-Hybrid System Techniques</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2003</creationdate><recordtype>article</recordtype><recordid>eNpFkElP5DAQRi3ECJrlyhFZQuKWHi9Z7CM0W0s9DNJwmDlZXsq0URKHOAH1v59At0Qdqr7Dq-_wEDqjZE5Jlf98NXb-i1Eiec4I2UMzSgTPeEH_7qMZIYxmkhXiEB2l9EqmySU9QIeU5ZJXVT5D5hE6KTq8TFjjRWy62EI74OjxsAb8D3Qa8J8utK4G_BSndR3dBuvW4duUJjLoGvvY48fR1qB7fBPeQwqx_ULuxs94gn54XSc43d1j9Hx3-7x4yFa_75eLq1Vm86IcMg_eggEhacGF86LQzlFaVDZnWriSFN54o4WoypJZgJwz50owxBSEVhL4Mbrc1nZ9fBshDaoJyUJd6xbimBQVpRRM8Amcb0Hbx5R68KrrQ6P7jaJEfUpVk1T1LXV6ON81j6YB943vLE7AxRZYh5f1R-hBmRDtGhrFKqEoVVJywf8DVfJ-Vw</recordid><startdate>20030314</startdate><enddate>20030314</enddate><creator>Nishikawa, Shuh-Ichi</creator><creator>Terazawa, Yumiko</creator><creator>Nakayama, Takeshi</creator><creator>Hirata, Aiko</creator><creator>Makio, Tadashi</creator><creator>Endo, Toshiya</creator><general>American Society for Biochemistry and Molecular Biology</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>8FD</scope><scope>FR3</scope><scope>M7N</scope><scope>P64</scope><scope>RC3</scope></search><sort><creationdate>20030314</creationdate><title>Nep98p Is a Component of the Yeast Spindle Pole Body and Essential for Nuclear Division and Fusion</title><author>Nishikawa, Shuh-Ichi ; Terazawa, Yumiko ; Nakayama, Takeshi ; Hirata, Aiko ; Makio, Tadashi ; Endo, Toshiya</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c456t-fefcebe891538df85add1157c42a8d605fbfba887662cee432dd6eb0b50179e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2003</creationdate><topic>Amino Acid Sequence</topic><topic>Cell Nucleus - metabolism</topic><topic>G2 Phase</topic><topic>Genes, Fungal</topic><topic>HSP70 Heat-Shock Proteins - metabolism</topic><topic>Membrane Proteins - chemistry</topic><topic>Membrane Proteins - metabolism</topic><topic>Membrane Proteins - physiology</topic><topic>Microscopy, Electron</topic><topic>Microscopy, Fluorescence</topic><topic>Mitosis</topic><topic>Molecular Chaperones</topic><topic>Molecular Sequence Data</topic><topic>Mutagenesis, Site-Directed</topic><topic>Mutation</topic><topic>Nuclear Proteins</topic><topic>Plasmids - metabolism</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - physiology</topic><topic>Spindle Apparatus</topic><topic>Temperature</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Nishikawa, Shuh-Ichi</creatorcontrib><creatorcontrib>Terazawa, Yumiko</creatorcontrib><creatorcontrib>Nakayama, Takeshi</creatorcontrib><creatorcontrib>Hirata, Aiko</creatorcontrib><creatorcontrib>Makio, Tadashi</creatorcontrib><creatorcontrib>Endo, Toshiya</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>Genetics Abstracts</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Nishikawa, Shuh-Ichi</au><au>Terazawa, Yumiko</au><au>Nakayama, Takeshi</au><au>Hirata, Aiko</au><au>Makio, Tadashi</au><au>Endo, Toshiya</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nep98p Is a Component of the Yeast Spindle Pole Body and Essential for Nuclear Division and Fusion</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2003-03-14</date><risdate>2003</risdate><volume>278</volume><issue>11</issue><spage>9938</spage><epage>9943</epage><pages>9938-9943</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>During the mating of yeast Saccharomyces cerevisiae , two haploid nuclei fuse to produce a diploid nucleus. This process requires the functions of BiP/Kar2p, a member of the
Hsp70 family in the endoplasmic reticulum, and its partner protein, Jem1p. To investigate further the role of BiP and Jem1p
in nuclear fusion, we screened for partner proteins for Jem1p by the yeast two-hybrid system and identified Nep98p. Nep98p
is an essential integral membrane protein of the nuclear envelope and is enriched in the spindle pole body (SPB), the sole
microtubule-organizing center in yeast. Temperature-sensitive nep98 mutant cells contain abnormal SPBs lacking the half-bridge, suggesting the essential role of Nep98p in the organization of
the normal SPB. Additionally, nep98 mutant cells show defects in mitotic nuclear division and nuclear fusion during mating. Because Jem1p is not required for
nuclear division, Nep98p probably has dual functions in Jem1p-dependent karyogamy and in Jem1p-independent nuclear division.</abstract><cop>United States</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>12493774</pmid><doi>10.1074/jbc.M210934200</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | The Journal of biological chemistry, 2003-03, Vol.278 (11), p.9938-9943 |
| issn | 0021-9258 1083-351X |
| language | eng |
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| source | ScienceDirect (Online service) |
| subjects | Amino Acid Sequence Cell Nucleus - metabolism G2 Phase Genes, Fungal HSP70 Heat-Shock Proteins - metabolism Membrane Proteins - chemistry Membrane Proteins - metabolism Membrane Proteins - physiology Microscopy, Electron Microscopy, Fluorescence Mitosis Molecular Chaperones Molecular Sequence Data Mutagenesis, Site-Directed Mutation Nuclear Proteins Plasmids - metabolism Protein Binding Protein Structure, Tertiary Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Saccharomyces cerevisiae Proteins - physiology Spindle Apparatus Temperature Two-Hybrid System Techniques |
| title | Nep98p Is a Component of the Yeast Spindle Pole Body and Essential for Nuclear Division and Fusion |
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