Nis1 encoded by YNL078W: A new neck protein of Saccharomyces cerevisiae
An uncharacterized gene, YNL078W, was isolated by the two-hybrid screening method using SHS1 (one of the septin genes) as bait and designated NISI (N eck protein Interacting with S Jeptins). Nisi interacts with all septins in the two-hy-brid assay system. Physical interaction between Nisi and Shsl i...
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| Veröffentlicht in: | Genes & Genetic Systems 2001, Vol.76(5), pp.335-343 |
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| creator | Iwase, M. (Tokyo Univ. (Japan)) Tohe, A |
| description | An uncharacterized gene, YNL078W, was isolated by the two-hybrid screening method using SHS1 (one of the septin genes) as bait and designated NISI (N eck protein Interacting with S Jeptins). Nisi interacts with all septins in the two-hy-brid assay system. Physical interaction between Nisi and Shsl in vivo was confirmed by a co-immunoprecipitation experiment. Neither disruption nor overexpression of NISI caused a prominent phenotypic change. NAP1 was isolated by two-hybrid screening using NIS1 as bait. We detected physical interaction between Nis1 and Nap1 in vivo by a co-immunoprecipitation experiment. Nis1 was found to bind Gin4 and Kcc4 in the two-hybrid assay. Thus, a number of the proteins interacting with Nis1 are members of the mitotic signaling network. The stable maintenance of Nisi was dependent on Napl. Nisi was phosphorylated throughout the cell cycle and was less abundant in G2/M phase. GFP-Nis1 is localized in the nucleus throughout the cell cycle and in the bud neck at G2/M phase in a septin-dependent manner. Altogether, the findings suggest that Nis1 may play a non-essential role in the mitotic signaling network. |
| doi_str_mv | 10.1266/ggs.76.335 |
| format | Article |
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(Tokyo Univ. (Japan)) ; Tohe, A</creator><creatorcontrib>Iwase, M. (Tokyo Univ. (Japan)) ; Tohe, A</creatorcontrib><description>An uncharacterized gene, YNL078W, was isolated by the two-hybrid screening method using SHS1 (one of the septin genes) as bait and designated NISI (N eck protein Interacting with S Jeptins). Nisi interacts with all septins in the two-hy-brid assay system. Physical interaction between Nisi and Shsl in vivo was confirmed by a co-immunoprecipitation experiment. Neither disruption nor overexpression of NISI caused a prominent phenotypic change. NAP1 was isolated by two-hybrid screening using NIS1 as bait. We detected physical interaction between Nis1 and Nap1 in vivo by a co-immunoprecipitation experiment. Nis1 was found to bind Gin4 and Kcc4 in the two-hybrid assay. Thus, a number of the proteins interacting with Nis1 are members of the mitotic signaling network. The stable maintenance of Nisi was dependent on Napl. Nisi was phosphorylated throughout the cell cycle and was less abundant in G2/M phase. GFP-Nis1 is localized in the nucleus throughout the cell cycle and in the bud neck at G2/M phase in a septin-dependent manner. Altogether, the findings suggest that Nis1 may play a non-essential role in the mitotic signaling network.</description><identifier>ISSN: 1341-7568</identifier><identifier>EISSN: 1880-5779</identifier><identifier>DOI: 10.1266/ggs.76.335</identifier><identifier>PMID: 11817649</identifier><language>eng</language><publisher>Japan: The Genetics Society of Japan</publisher><subject>Carrier Proteins - metabolism ; Cell Cycle Proteins - metabolism ; Cyclin-Dependent Kinases - metabolism ; Cytoskeletal Proteins ; DNA ; DNA-Binding Proteins - metabolism ; Ferrochelatase - genetics ; GENES ; Green Fluorescent Proteins ; Hydroxyurea - pharmacology ; IMMUNOPRECIPITATION TESTS ; Luminescent Proteins ; Mating Factor ; Mitosis - drug effects ; NAP1 gene ; NIS1 gene ; Nocodazole - pharmacology ; Nuclear Proteins - metabolism ; Nucleic Acid Synthesis Inhibitors - pharmacology ; Peptides - pharmacology ; Phosphorylation ; Protein Binding ; Protein Kinases - metabolism ; Recombinant Fusion Proteins - metabolism ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - metabolism ; Saccharomyces cerevisiae Proteins - metabolism ; SELECTION ; YNL078W gene</subject><ispartof>Genes & Genetic Systems, 2001, Vol.76(5), pp.335-343</ispartof><rights>2001 by The Genetics Society of Japan</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c576t-740fdf2e3a5163862b5a73d38074af2407b55d2be0d8ed792420cd5f4d7cafdd3</citedby><cites>FETCH-LOGICAL-c576t-740fdf2e3a5163862b5a73d38074af2407b55d2be0d8ed792420cd5f4d7cafdd3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1883,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/11817649$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Iwase, M. (Tokyo Univ. (Japan))</creatorcontrib><creatorcontrib>Tohe, A</creatorcontrib><title>Nis1 encoded by YNL078W: A new neck protein of Saccharomyces cerevisiae</title><title>Genes & Genetic Systems</title><addtitle>Genes Genet. Syst.</addtitle><description>An uncharacterized gene, YNL078W, was isolated by the two-hybrid screening method using SHS1 (one of the septin genes) as bait and designated NISI (N eck protein Interacting with S Jeptins). Nisi interacts with all septins in the two-hy-brid assay system. Physical interaction between Nisi and Shsl in vivo was confirmed by a co-immunoprecipitation experiment. Neither disruption nor overexpression of NISI caused a prominent phenotypic change. NAP1 was isolated by two-hybrid screening using NIS1 as bait. We detected physical interaction between Nis1 and Nap1 in vivo by a co-immunoprecipitation experiment. Nis1 was found to bind Gin4 and Kcc4 in the two-hybrid assay. Thus, a number of the proteins interacting with Nis1 are members of the mitotic signaling network. The stable maintenance of Nisi was dependent on Napl. Nisi was phosphorylated throughout the cell cycle and was less abundant in G2/M phase. GFP-Nis1 is localized in the nucleus throughout the cell cycle and in the bud neck at G2/M phase in a septin-dependent manner. 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(Japan)) ; Tohe, A</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c576t-740fdf2e3a5163862b5a73d38074af2407b55d2be0d8ed792420cd5f4d7cafdd3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2001</creationdate><topic>Carrier Proteins - metabolism</topic><topic>Cell Cycle Proteins - metabolism</topic><topic>Cyclin-Dependent Kinases - metabolism</topic><topic>Cytoskeletal Proteins</topic><topic>DNA</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Ferrochelatase - genetics</topic><topic>GENES</topic><topic>Green Fluorescent Proteins</topic><topic>Hydroxyurea - pharmacology</topic><topic>IMMUNOPRECIPITATION TESTS</topic><topic>Luminescent Proteins</topic><topic>Mating Factor</topic><topic>Mitosis - drug effects</topic><topic>NAP1 gene</topic><topic>NIS1 gene</topic><topic>Nocodazole - pharmacology</topic><topic>Nuclear Proteins - metabolism</topic><topic>Nucleic Acid Synthesis Inhibitors - pharmacology</topic><topic>Peptides - pharmacology</topic><topic>Phosphorylation</topic><topic>Protein Binding</topic><topic>Protein Kinases - metabolism</topic><topic>Recombinant Fusion Proteins - metabolism</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>SELECTION</topic><topic>YNL078W gene</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iwase, M. (Tokyo Univ. (Japan))</creatorcontrib><creatorcontrib>Tohe, A</creatorcontrib><collection>AGRIS</collection><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><collection>MEDLINE - Academic</collection><jtitle>Genes & Genetic Systems</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iwase, M. (Tokyo Univ. (Japan))</au><au>Tohe, A</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Nis1 encoded by YNL078W: A new neck protein of Saccharomyces cerevisiae</atitle><jtitle>Genes & Genetic Systems</jtitle><addtitle>Genes Genet. Syst.</addtitle><date>2001-10-01</date><risdate>2001</risdate><volume>76</volume><issue>5</issue><spage>335</spage><epage>343</epage><pages>335-343</pages><issn>1341-7568</issn><eissn>1880-5779</eissn><abstract>An uncharacterized gene, YNL078W, was isolated by the two-hybrid screening method using SHS1 (one of the septin genes) as bait and designated NISI (N eck protein Interacting with S Jeptins). Nisi interacts with all septins in the two-hy-brid assay system. Physical interaction between Nisi and Shsl in vivo was confirmed by a co-immunoprecipitation experiment. Neither disruption nor overexpression of NISI caused a prominent phenotypic change. NAP1 was isolated by two-hybrid screening using NIS1 as bait. We detected physical interaction between Nis1 and Nap1 in vivo by a co-immunoprecipitation experiment. Nis1 was found to bind Gin4 and Kcc4 in the two-hybrid assay. Thus, a number of the proteins interacting with Nis1 are members of the mitotic signaling network. The stable maintenance of Nisi was dependent on Napl. Nisi was phosphorylated throughout the cell cycle and was less abundant in G2/M phase. GFP-Nis1 is localized in the nucleus throughout the cell cycle and in the bud neck at G2/M phase in a septin-dependent manner. Altogether, the findings suggest that Nis1 may play a non-essential role in the mitotic signaling network.</abstract><cop>Japan</cop><pub>The Genetics Society of Japan</pub><pmid>11817649</pmid><doi>10.1266/ggs.76.335</doi><tpages>9</tpages><oa>free_for_read</oa></addata></record> |
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| ispartof | Genes & Genetic Systems, 2001, Vol.76(5), pp.335-343 |
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| source | MEDLINE; J-STAGE (Japan Science & Technology Information Aggregator, Electronic) Freely Available Titles - Japanese; EZB-FREE-00999 freely available EZB journals |
| subjects | Carrier Proteins - metabolism Cell Cycle Proteins - metabolism Cyclin-Dependent Kinases - metabolism Cytoskeletal Proteins DNA DNA-Binding Proteins - metabolism Ferrochelatase - genetics GENES Green Fluorescent Proteins Hydroxyurea - pharmacology IMMUNOPRECIPITATION TESTS Luminescent Proteins Mating Factor Mitosis - drug effects NAP1 gene NIS1 gene Nocodazole - pharmacology Nuclear Proteins - metabolism Nucleic Acid Synthesis Inhibitors - pharmacology Peptides - pharmacology Phosphorylation Protein Binding Protein Kinases - metabolism Recombinant Fusion Proteins - metabolism SACCHAROMYCES CEREVISIAE Saccharomyces cerevisiae - genetics Saccharomyces cerevisiae - metabolism Saccharomyces cerevisiae Proteins - metabolism SELECTION YNL078W gene |
| title | Nis1 encoded by YNL078W: A new neck protein of Saccharomyces cerevisiae |
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