IRIS publication 40838341
A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a type III topology.
RIS format for Endnote and similar
TY - JOUR - Clarke, D. J.,Jacq, A.,Holland, I. B. - 1996 - June - A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a type III topology. - Validated - () - 20 - 6 - 1273 - 86 - We describe a novel Escherichia coli protein, DjlA, containing a highly conserved J-region motif, which is present in the DnaJ protein chaperone family and required for interaction with DnaK. Remarkably, DjlA is shown to be a membrane protein, localized to the inner membrane with the unusual Type III topology (N-out, C-in). Thus, DjlA appears to present an extremely short N-terminus to the periplasm and has a single transmembrane domain (TMD) and a large cytoplasmic domain containing the C-terminal J-region. Analysis of the TMD of DjlA and recently identified homologues in Coxiella burnetti and Haemophilus influenzae revealed a striking pattern of conserved glycines (or rarely alanine), with a four-residue spacing. This motif, predicted to form a spiral groove in the TMD, is more marked than a repeating glycine motif, implicated in the dimerization of TMDs of some eukaryotic proteins. This feature of DjlA could represent a promiscuous docking mechanism for interaction with a variety of membrane proteins. DjlA null mutants can be isolated but these appear rapidly to accumulate suppressors to correct envelope and growth defects. Moderate (10-fold) overproduction of DjlA suppresses a mutation in FtsZ but markedly perturbs cell division and cell-envelope growth in minimal medium. We propose that DjlA plays a role in the correct assembly, activity and/or maintenance of a number of membrane proteins, including two-component signal-transduction systems. - 0950-382X (Print) 0950-38 DA - 1996/06 ER -
BIBTeX format for JabRef and similar
@article{V40838341, = {Clarke, D. J. and Jacq, A. and Holland, I. B. }, = {1996}, = {June}, = {A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a type III topology.}, = {Validated}, = {()}, = {20}, = {6}, pages = {1273--86}, = {{We describe a novel Escherichia coli protein, DjlA, containing a highly conserved J-region motif, which is present in the DnaJ protein chaperone family and required for interaction with DnaK. Remarkably, DjlA is shown to be a membrane protein, localized to the inner membrane with the unusual Type III topology (N-out, C-in). Thus, DjlA appears to present an extremely short N-terminus to the periplasm and has a single transmembrane domain (TMD) and a large cytoplasmic domain containing the C-terminal J-region. Analysis of the TMD of DjlA and recently identified homologues in Coxiella burnetti and Haemophilus influenzae revealed a striking pattern of conserved glycines (or rarely alanine), with a four-residue spacing. This motif, predicted to form a spiral groove in the TMD, is more marked than a repeating glycine motif, implicated in the dimerization of TMDs of some eukaryotic proteins. This feature of DjlA could represent a promiscuous docking mechanism for interaction with a variety of membrane proteins. DjlA null mutants can be isolated but these appear rapidly to accumulate suppressors to correct envelope and growth defects. Moderate (10-fold) overproduction of DjlA suppresses a mutation in FtsZ but markedly perturbs cell division and cell-envelope growth in minimal medium. We propose that DjlA plays a role in the correct assembly, activity and/or maintenance of a number of membrane proteins, including two-component signal-transduction systems.}}, issn = {0950-382X (Print) 0950-38}, source = {IRIS} }
Data as stored in IRIS
AUTHORS | Clarke, D. J.,Jacq, A.,Holland, I. B. | ||
YEAR | 1996 | ||
MONTH | June | ||
JOURNAL_CODE | |||
TITLE | A novel DnaJ-like protein in Escherichia coli inserts into the cytoplasmic membrane with a type III topology. | ||
STATUS | Validated | ||
TIMES_CITED | () | ||
SEARCH_KEYWORD | |||
VOLUME | 20 | ||
ISSUE | 6 | ||
START_PAGE | 1273 | ||
END_PAGE | 86 | ||
ABSTRACT | We describe a novel Escherichia coli protein, DjlA, containing a highly conserved J-region motif, which is present in the DnaJ protein chaperone family and required for interaction with DnaK. Remarkably, DjlA is shown to be a membrane protein, localized to the inner membrane with the unusual Type III topology (N-out, C-in). Thus, DjlA appears to present an extremely short N-terminus to the periplasm and has a single transmembrane domain (TMD) and a large cytoplasmic domain containing the C-terminal J-region. Analysis of the TMD of DjlA and recently identified homologues in Coxiella burnetti and Haemophilus influenzae revealed a striking pattern of conserved glycines (or rarely alanine), with a four-residue spacing. This motif, predicted to form a spiral groove in the TMD, is more marked than a repeating glycine motif, implicated in the dimerization of TMDs of some eukaryotic proteins. This feature of DjlA could represent a promiscuous docking mechanism for interaction with a variety of membrane proteins. DjlA null mutants can be isolated but these appear rapidly to accumulate suppressors to correct envelope and growth defects. Moderate (10-fold) overproduction of DjlA suppresses a mutation in FtsZ but markedly perturbs cell division and cell-envelope growth in minimal medium. We propose that DjlA plays a role in the correct assembly, activity and/or maintenance of a number of membrane proteins, including two-component signal-transduction systems. | ||
PUBLISHER_LOCATION | |||
ISBN_ISSN | 0950-382X (Print) 0950-38 | ||
EDITION | |||
URL | |||
DOI_LINK | |||
FUNDING_BODY | |||
GRANT_DETAILS |