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PMID: 10400580 Published · ppublish English Journal Article

The unique chaperone operon of Thermotoga maritima: cloning and initial characterization of a functional Hsp70 and small heat shock protein.

Journal of bacteriology ·Vol. 181 ·No. 14 ·1999-07-00 ·Pages 4237-44

Michelini ET, Flynn GC

Abstract

The hyperthermophilic eubacterium Thermotoga maritima possesses an operon encoding an Hsp70 molecular chaperone protein and a protein with meaningful homology to the small heat shock protein family of chaperones. This represents the first demonstrated co-operon organization for these two important classes of molecular chaperones. We have cloned and initially characterized these proteins as functional chaperones in vitro: the Hsp70 is capable of ATP hydrolysis and substrate binding, and the small heat shock protein can suppress protein aggregation and stably bind a refolding-competent substrate. In addition, the primary sequence of the Hsp70 is used to infer the phylogenetic relationships of T. maritima, one of the deepest-branching eubacteria known.

MeSH Terms
Adenosine Triphosphatases/metabolism Adenosine Triphosphate/metabolism Cloning, Molecular DNA, Bacterial/genetics HSP70 Heat-Shock Proteins/chemistry,genetics,isolation & purification,metabolism Heat-Shock Proteins/chemistry,genetics,isolation & purification,metabolism Molecular Chaperones/chemistry,genetics,isolation & purification,metabolism Operon/genetics Peptides/metabolism Phylogeny Thermotoga maritima/genetics,metabolism
Chemicals
DNA, Bacterial HSP70 Heat-Shock Proteins Heat-Shock Proteins Molecular Chaperones Peptides Adenosine Triphosphate Adenosine Triphosphatases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Michelini E T
Institute of Molecular Biology and Department of Chemistry, University of Oregon, Eugene, Oregon 97403, USA.
Flynn G C
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Article Info
Journal
Journal of bacteriology
Abbr.
J Bacteriol
ISSN
0021-9193
DOI
10.1128/JB.181.14.4237-4244.1999
Published
1999-07-00
Pages
4237-44
Language
English
Region
United States
NLM ID
2985120R
PMCID
PMC93924
Subset
IM
External Links
PubMed source DOI: 10.1128/JB.181.14.4237-4244.1999 PMC Full Text View journal details
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