BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin

BIK1 function is required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. The BIK1 protein colocalizes with tubulin to the spindle pole body and mitotic spindle. Synthetic lethality observed in double mutant strains containing a mutation in the BIK1 gene and in th...

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Veröffentlicht in:The Journal of cell biology 1990-12, Vol.111 (6), p.2573-2586
Hauptverfasser: Berlin, V. (Vertex Pharmaceuticals, Cambridge, MA), Styles, C.A, Fink, G.R
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container_title The Journal of cell biology
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creator Berlin, V. (Vertex Pharmaceuticals, Cambridge, MA)
Styles, C.A
Fink, G.R
description BIK1 function is required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. The BIK1 protein colocalizes with tubulin to the spindle pole body and mitotic spindle. Synthetic lethality observed in double mutant strains containing a mutation in the BIK1 gene and in the gene for α- or β-tubulin is consistent with a physical interaction between BIK1 and tubulin. Furthermore, over- or underexpression of BIK1 causes aberrant microtubule assembly and function. bik1 null mutants are viable but contain very short or undetectable cytoplasmic microtubules. Spindle formation often occurs strictly within the mother cell, probably accounting for the many multinucleate and anucleate bik1 cells. Elevated levels of chromosome loss in bik1 cells are indicative of defective spindle function. Nuclear fusion is blocked in bik1 × bik1 zygotes, which have truncated cytoplasmic microtubules. Cells overexpressing BIK1 initially have abnormally short or nonexistent spindle microtubules and long cytoplasmic microtubules. Subsequently, cells lose all microtubule structures, coincident with the arrest of division. Based on these results, we propose that BIK1 is required stoichiometrically for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation.
doi_str_mv 10.1083/jcb.111.6.2573
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(Vertex Pharmaceuticals, Cambridge, MA) ; Styles, C.A ; Fink, G.R</creator><creatorcontrib>Berlin, V. (Vertex Pharmaceuticals, Cambridge, MA) ; Styles, C.A ; Fink, G.R</creatorcontrib><description>BIK1 function is required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. The BIK1 protein colocalizes with tubulin to the spindle pole body and mitotic spindle. Synthetic lethality observed in double mutant strains containing a mutation in the BIK1 gene and in the gene for α- or β-tubulin is consistent with a physical interaction between BIK1 and tubulin. Furthermore, over- or underexpression of BIK1 causes aberrant microtubule assembly and function. bik1 null mutants are viable but contain very short or undetectable cytoplasmic microtubules. Spindle formation often occurs strictly within the mother cell, probably accounting for the many multinucleate and anucleate bik1 cells. Elevated levels of chromosome loss in bik1 cells are indicative of defective spindle function. Nuclear fusion is blocked in bik1 × bik1 zygotes, which have truncated cytoplasmic microtubules. Cells overexpressing BIK1 initially have abnormally short or nonexistent spindle microtubules and long cytoplasmic microtubules. Subsequently, cells lose all microtubule structures, coincident with the arrest of division. 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Biological and molecular evolution ; Genotype ; GLICOPROTEINAS ; GLYCOPROTEINE ; GLYCOPROTEINS ; Microtubules ; Microtubules - physiology ; MITOSE ; MITOSIS ; MOLECULAR SEQUENCE DATA ; Mother cells ; Mutation ; Plasmids ; Promoter Regions, Genetic ; Protein Conformation ; PROTEINAS ; PROTEINE ; PROTEINS ; Recombination, Genetic ; SACCHAROMYCES CEREVISIAE ; Saccharomyces cerevisiae - cytology ; Saccharomyces cerevisiae - genetics ; Saccharomyces cerevisiae - physiology ; Sequence Homology, Nucleic Acid ; Spindle pole body ; Thallophyta, bryophyta ; Tubulin - genetics ; Tubulin - isolation &amp; purification ; Vegetals ; Yeasts</subject><ispartof>The Journal of cell biology, 1990-12, Vol.111 (6), p.2573-2586</ispartof><rights>Copyright 1990 The Rockefeller University Press</rights><rights>1991 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c455t-1762b1949537b9c78a434cd6f115b4048562b6e69dbef647c62a23520225622d3</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>230,314,780,784,885,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&amp;idt=19600447$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/2277073$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Berlin, V. (Vertex Pharmaceuticals, Cambridge, MA)</creatorcontrib><creatorcontrib>Styles, C.A</creatorcontrib><creatorcontrib>Fink, G.R</creatorcontrib><title>BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin</title><title>The Journal of cell biology</title><addtitle>J Cell Biol</addtitle><description>BIK1 function is required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. The BIK1 protein colocalizes with tubulin to the spindle pole body and mitotic spindle. Synthetic lethality observed in double mutant strains containing a mutation in the BIK1 gene and in the gene for α- or β-tubulin is consistent with a physical interaction between BIK1 and tubulin. Furthermore, over- or underexpression of BIK1 causes aberrant microtubule assembly and function. bik1 null mutants are viable but contain very short or undetectable cytoplasmic microtubules. Spindle formation often occurs strictly within the mother cell, probably accounting for the many multinucleate and anucleate bik1 cells. Elevated levels of chromosome loss in bik1 cells are indicative of defective spindle function. Nuclear fusion is blocked in bik1 × bik1 zygotes, which have truncated cytoplasmic microtubules. Cells overexpressing BIK1 initially have abnormally short or nonexistent spindle microtubules and long cytoplasmic microtubules. Subsequently, cells lose all microtubule structures, coincident with the arrest of division. Based on these results, we propose that BIK1 is required stoichiometrically for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation.</description><subject>Amino Acid Sequence</subject><subject>AMINO ACID SEQUENCES</subject><subject>Animals</subject><subject>Antibodies</subject><subject>Biological and medical sciences</subject><subject>Cell cycle</subject><subject>Cell Division</subject><subject>Cells</subject><subject>Chromosomes, Fungal</subject><subject>Classical genetics, quantitative genetics, hybrids</subject><subject>CONJUGATION</subject><subject>Crosses, Genetic</subject><subject>Daughter cells</subject><subject>Diploidy</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - metabolism</subject><subject>Genes, Fungal</subject><subject>Genetics of eukaryotes. Biological and molecular evolution</subject><subject>Genotype</subject><subject>GLICOPROTEINAS</subject><subject>GLYCOPROTEINE</subject><subject>GLYCOPROTEINS</subject><subject>Microtubules</subject><subject>Microtubules - physiology</subject><subject>MITOSE</subject><subject>MITOSIS</subject><subject>MOLECULAR SEQUENCE DATA</subject><subject>Mother cells</subject><subject>Mutation</subject><subject>Plasmids</subject><subject>Promoter Regions, Genetic</subject><subject>Protein Conformation</subject><subject>PROTEINAS</subject><subject>PROTEINE</subject><subject>PROTEINS</subject><subject>Recombination, Genetic</subject><subject>SACCHAROMYCES CEREVISIAE</subject><subject>Saccharomyces cerevisiae - cytology</subject><subject>Saccharomyces cerevisiae - genetics</subject><subject>Saccharomyces cerevisiae - physiology</subject><subject>Sequence Homology, Nucleic Acid</subject><subject>Spindle pole body</subject><subject>Thallophyta, bryophyta</subject><subject>Tubulin - genetics</subject><subject>Tubulin - isolation &amp; purification</subject><subject>Vegetals</subject><subject>Yeasts</subject><issn>0021-9525</issn><issn>1540-8140</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1990</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpVkUtv1DAUhS0EKkNhywKB5E1ZNcHXz8mmEq14VFRiUbq2HMeZ8Sixp3ZSVHb8czzMqIXVle537rF1DkKvgdRAluzDxrY1ANSypkKxJ2gBgpNqCZw8RQtCKFSNoOI5epHzhhDCFWdH6IhSpYhiC_T7_PIbnGKDtylOzgec3O3sk-twHxMevS3ruZ0Hh_s52MnHgLs5-bDCo5l2w4SuyKaYfcbl_NpYuzYpjvfWZWxdcnc-e-NOsY1DtGbwv8r-p5_W-K-vDy_Rs94M2b06zGN08_nTj4uv1dX3L5cXH68qy4WYKlCSttDwRjDVNlYtDWfcdrIHEC0nfCkKl042Xet6yZWV1FAmKKG0ENqxY3S2993O7eg668KUzKC3yY8m3etovP6fBL_Wq3inKYDkBIrB-4NBirezy5MefbZuGExwcc56SSiTpGFFWO-FJbyck-sfHgGid6XpUpoupWmpd6WVg3f_fu1Bfmip8JMDN7lE2CcTrM-Pro0sxXJVdG_3uk2eYnrkEnhJouA3e9ybqM0qFYub6waAcMHZH0D5s0Q</recordid><startdate>19901201</startdate><enddate>19901201</enddate><creator>Berlin, V. 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(Vertex Pharmaceuticals, Cambridge, MA) ; Styles, C.A ; Fink, G.R</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c455t-1762b1949537b9c78a434cd6f115b4048562b6e69dbef647c62a23520225622d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1990</creationdate><topic>Amino Acid Sequence</topic><topic>AMINO ACID SEQUENCES</topic><topic>Animals</topic><topic>Antibodies</topic><topic>Biological and medical sciences</topic><topic>Cell cycle</topic><topic>Cell Division</topic><topic>Cells</topic><topic>Chromosomes, Fungal</topic><topic>Classical genetics, quantitative genetics, hybrids</topic><topic>CONJUGATION</topic><topic>Crosses, Genetic</topic><topic>Daughter cells</topic><topic>Diploidy</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - metabolism</topic><topic>Genes, Fungal</topic><topic>Genetics of eukaryotes. Biological and molecular evolution</topic><topic>Genotype</topic><topic>GLICOPROTEINAS</topic><topic>GLYCOPROTEINE</topic><topic>GLYCOPROTEINS</topic><topic>Microtubules</topic><topic>Microtubules - physiology</topic><topic>MITOSE</topic><topic>MITOSIS</topic><topic>MOLECULAR SEQUENCE DATA</topic><topic>Mother cells</topic><topic>Mutation</topic><topic>Plasmids</topic><topic>Promoter Regions, Genetic</topic><topic>Protein Conformation</topic><topic>PROTEINAS</topic><topic>PROTEINE</topic><topic>PROTEINS</topic><topic>Recombination, Genetic</topic><topic>SACCHAROMYCES CEREVISIAE</topic><topic>Saccharomyces cerevisiae - cytology</topic><topic>Saccharomyces cerevisiae - genetics</topic><topic>Saccharomyces cerevisiae - physiology</topic><topic>Sequence Homology, Nucleic Acid</topic><topic>Spindle pole body</topic><topic>Thallophyta, bryophyta</topic><topic>Tubulin - genetics</topic><topic>Tubulin - isolation &amp; purification</topic><topic>Vegetals</topic><topic>Yeasts</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Berlin, V. (Vertex Pharmaceuticals, Cambridge, MA)</creatorcontrib><creatorcontrib>Styles, C.A</creatorcontrib><creatorcontrib>Fink, G.R</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>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>The Journal of cell biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Berlin, V. (Vertex Pharmaceuticals, Cambridge, MA)</au><au>Styles, C.A</au><au>Fink, G.R</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin</atitle><jtitle>The Journal of cell biology</jtitle><addtitle>J Cell Biol</addtitle><date>1990-12-01</date><risdate>1990</risdate><volume>111</volume><issue>6</issue><spage>2573</spage><epage>2586</epage><pages>2573-2586</pages><issn>0021-9525</issn><eissn>1540-8140</eissn><coden>JCLBA3</coden><abstract>BIK1 function is required for nuclear fusion, chromosome disjunction, and nuclear segregation during mitosis. The BIK1 protein colocalizes with tubulin to the spindle pole body and mitotic spindle. Synthetic lethality observed in double mutant strains containing a mutation in the BIK1 gene and in the gene for α- or β-tubulin is consistent with a physical interaction between BIK1 and tubulin. Furthermore, over- or underexpression of BIK1 causes aberrant microtubule assembly and function. bik1 null mutants are viable but contain very short or undetectable cytoplasmic microtubules. Spindle formation often occurs strictly within the mother cell, probably accounting for the many multinucleate and anucleate bik1 cells. Elevated levels of chromosome loss in bik1 cells are indicative of defective spindle function. Nuclear fusion is blocked in bik1 × bik1 zygotes, which have truncated cytoplasmic microtubules. Cells overexpressing BIK1 initially have abnormally short or nonexistent spindle microtubules and long cytoplasmic microtubules. Subsequently, cells lose all microtubule structures, coincident with the arrest of division. Based on these results, we propose that BIK1 is required stoichiometrically for the formation or stabilization of microtubules during mitosis and for spindle pole body fusion during conjugation.</abstract><cop>New York, NY</cop><pub>Rockefeller University Press</pub><pmid>2277073</pmid><doi>10.1083/jcb.111.6.2573</doi><tpages>14</tpages><oa>free_for_read</oa></addata></record>
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identifier ISSN: 0021-9525
ispartof The Journal of cell biology, 1990-12, Vol.111 (6), p.2573-2586
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source MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection
subjects Amino Acid Sequence
AMINO ACID SEQUENCES
Animals
Antibodies
Biological and medical sciences
Cell cycle
Cell Division
Cells
Chromosomes, Fungal
Classical genetics, quantitative genetics, hybrids
CONJUGATION
Crosses, Genetic
Daughter cells
Diploidy
Fundamental and applied biological sciences. Psychology
Fungal Proteins - metabolism
Genes, Fungal
Genetics of eukaryotes. Biological and molecular evolution
Genotype
GLICOPROTEINAS
GLYCOPROTEINE
GLYCOPROTEINS
Microtubules
Microtubules - physiology
MITOSE
MITOSIS
MOLECULAR SEQUENCE DATA
Mother cells
Mutation
Plasmids
Promoter Regions, Genetic
Protein Conformation
PROTEINAS
PROTEINE
PROTEINS
Recombination, Genetic
SACCHAROMYCES CEREVISIAE
Saccharomyces cerevisiae - cytology
Saccharomyces cerevisiae - genetics
Saccharomyces cerevisiae - physiology
Sequence Homology, Nucleic Acid
Spindle pole body
Thallophyta, bryophyta
Tubulin - genetics
Tubulin - isolation & purification
Vegetals
Yeasts
title BIK1, a protein required for microtubule function during mating and mitosis in Saccharomyces cerevisiae, colocalizes with tubulin
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