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PMID: 7744969 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

A yeast DnaJ homologue, Scj1p, can function in the endoplasmic reticulum with BiP/Kar2p via a conserved domain that specifies interactions with Hsp70s.

The Journal of cell biology ·Vol. 129 ·No. 4 ·1995-05-00 ·Pages 979-88

Schlenstedt G, Harris S, Risse B, Lill R, Silver PA

Abstract

Eukaryotic cells contain multiple Hsp70 proteins and DnaJ homologues. The partnership between a given Hsp70 and its interacting DnaJ could, in principle, be determined by their cellular colocalization or by specific protein-protein interactions. The yeast SCJ1 gene encodes one of several homologues of the bacterial chaperone DnaJ. We show that Scj1p is located in the lumen of the endoplasmic reticulum (ER), where it can function with Kar2p (the ER-lumenal BiP/Hsp70 of yeast). The region common to all DnaJ homologues (termed the J domain) from Scj1p can be swapped for a similar region in Sec63p, which is known to interact with Kar2p in the ER lumen, to form a functional transmembrane protein component of the secretory machinery. Thus, Kar2p can interact with two different DnaJ proteins. On the other hand, J domains from two other non-ER DnaJs, Sis1p and Mdj1p, do not function when swapped into Sec63p. However, only three amino acid changes in the Sis1p J domain render the Sec63 fusion protein fully functional in the ER lumen. These results indicate that the choice of an Hsp70 partner by a given DnaJ homologue is specified by the J domain.

Related Genes
MeSH Terms
Amino Acid Sequence Base Sequence Cell Compartmentation Conserved Sequence Endoplasmic Reticulum/metabolism Fluorescent Antibody Technique Fungal Proteins/genetics,metabolism HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins/metabolism Heat-Shock Proteins/genetics,metabolism Membrane Proteins/genetics,metabolism Membrane Transport Proteins Molecular Sequence Data Protein Binding Saccharomyces cerevisiae/genetics,metabolism Saccharomyces cerevisiae Proteins Sequence Homology, Amino Acid Structure-Activity Relationship
Chemicals
Fungal Proteins HSP40 Heat-Shock Proteins HSP70 Heat-Shock Proteins Heat-Shock Proteins KAR2 protein, yeast Membrane Proteins Membrane Transport Proteins SCJ1 protein, S cerevisiae SEC63 protein, S cerevisiae Saccharomyces cerevisiae Proteins
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Schlenstedt G
Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
Harris S
Risse B
Lill R
Silver P A
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Article Info
Journal
The Journal of cell biology
Abbr.
J Cell Biol
ISSN
0021-9525
Published
1995-05-00
Pages
979-88
Language
English
Region
United States
NLM ID
0375356
PMCID
PMC2120480
Subset
IM
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