Literature DB >> 9148890

The yeast JEM1p is a DnaJ-like protein of the endoplasmic reticulum membrane required for nuclear fusion.

S Nishikawa1, T Endo.   

Abstract

DnaJ-like proteins are functional partners for Hsp70 molecular chaperones. Complete nucleotide sequencing of yeast chromosome X has revealed that an open reading frame YJL073w encodes a novel member of the DnaJ-like protein family. The open reading frame represents a protein of 692 amino acids with a J-domain and one putative membrane-spanning segment. An epitope-tagged version of the protein was anchored in the endoplasmic reticulum (ER) membrane and its J-domain faced the ER lumen. We therefore propose to designate this gene JEM1 (DnaJ-like protein of the ER membrane) and to designate its gene product JEM1p. The JEM1 gene is not essential for cell growth, but double disruption of the JEM1 gene and the SCJ1 gene, which encodes another DnaJ-like protein in the ER lumen, causes growth arrest at elevated temperature. The Deltajem1 mutant is defective in nuclear fusion, karyogamy, during mating. A mutant JEM1p carrying a mutation in the highly conserved His-Pro-Asp sequence in the J-domain could not complement either temperature-sensitive growth of the Deltajem1 Deltascj1 double mutant or defects in karyogamy of the Deltajem1 mutant. JEM1p likely assists the functions of BiP, Hsp70 in the ER, including karyogamy.

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Year:  1997        PMID: 9148890     DOI: 10.1074/jbc.272.20.12889

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  35 in total

1.  Proteins of the endoplasmic-reticulum-associated degradation pathway: domain detection and function prediction.

Authors:  C P Ponting
Journal:  Biochem J       Date:  2000-10-15       Impact factor: 3.857

2.  Evidence for control of nitrogen metabolism by a START-dependent mechanism in Saccharomyces cerevisiae.

Authors:  B A Bryan; E McGrew; Y Lu; M Polymenis
Journal:  Mol Genet Genomics       Date:  2003-11-27       Impact factor: 3.291

3.  J domain co-chaperone specificity defines the role of BiP during protein translocation.

Authors:  Shruthi S Vembar; Martin C Jonikas; Linda M Hendershot; Jonathan S Weissman; Jeffrey L Brodsky
Journal:  J Biol Chem       Date:  2010-04-29       Impact factor: 5.157

4.  ERdj3, a stress-inducible endoplasmic reticulum DnaJ homologue, serves as a cofactor for BiP's interactions with unfolded substrates.

Authors:  Ying Shen; Linda M Hendershot
Journal:  Mol Biol Cell       Date:  2004-11-03       Impact factor: 4.138

Review 5.  The Malleable Nature of the Budding Yeast Nuclear Envelope: Flares, Fusion, and Fenestrations.

Authors:  Rebecca A Meseroll; Orna Cohen-Fix
Journal:  J Cell Physiol       Date:  2016-04-08       Impact factor: 6.384

6.  Specific molecular chaperone interactions and an ATP-dependent conformational change are required during posttranslational protein translocation into the yeast ER.

Authors:  A J McClellan; J B Endres; J P Vogel; D Palazzi; M D Rose; J L Brodsky
Journal:  Mol Biol Cell       Date:  1998-12       Impact factor: 4.138

7.  Analysis of ER resident proteins in Saccharomyces cerevisiae: implementation of H/KDEL retrieval sequences.

Authors:  Carissa L Young; David L Raden; Anne S Robinson
Journal:  Traffic       Date:  2013-02-04       Impact factor: 6.215

8.  Prm3p is a pheromone-induced peripheral nuclear envelope protein required for yeast nuclear fusion.

Authors:  Shu Shen; Cynthia E Tobery; Mark D Rose
Journal:  Mol Biol Cell       Date:  2009-03-18       Impact factor: 4.138

9.  The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human homologue interacts with alpha1-antichymotrypsin and kinetically interferes with its serpin inhibitory activity.

Authors:  Barbara Kroczynska; Christina M Evangelista; Shalaka S Samant; Ebrahim C Elguindi; Sylvie Y Blond
Journal:  J Biol Chem       Date:  2003-12-10       Impact factor: 5.157

10.  The endoplasmic reticulum-associated degradation of the epithelial sodium channel requires a unique complement of molecular chaperones.

Authors:  Teresa M Buck; Alexander R Kolb; Cary R Boyd; Thomas R Kleyman; Jeffrey L Brodsky
Journal:  Mol Biol Cell       Date:  2010-01-28       Impact factor: 4.138

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