A5012242924- Protein Structure and Dynamics
- Heat shock proteins research
- Endoplasmic Reticulum Stress and Disease
- Enzyme Structure and Function
- Redox biology and oxidative stress
- Bacterial Genetics and Biotechnology
- RNA and protein synthesis mechanisms
- RNA Research and Splicing
- Toxin Mechanisms and Immunotoxins
- RNA modifications and cancer
- Photosynthetic Processes and Mechanisms
- Glycosylation and Glycoproteins Research
- Mitochondrial Function and Pathology
- thermodynamics and calorimetric analyses
- Hemoglobin structure and function
- Fungal and yeast genetics research
- Bacteriophages and microbial interactions
- Transgenic Plants and Applications
- Monoclonal and Polyclonal Antibodies Research
- Escherichia coli research studies
- Metalloenzymes and iron-sulfur proteins
- Microbial Metabolic Engineering and Bioproduction
- Biochemical and Structural Characterization
- Adenosine and Purinergic Signaling
- Alzheimer's disease research and treatments
Howard Hughes Medical Institute
2016-2025
University of Michigan
2016-2025
Ann Arbor Center for Independent Living
2011-2017
Michigan United
2014
Institut thématique Génétique, génomique et bioinformatique
1984-2011
Harvard University
1991-2004
The University of Texas at Austin
1990-2004
Oklahoma State University
2003
University of Auckland
2001
University of Regensburg
1993-1995
The Escherichia coli dnaK gene is homologous to the major heat shock-induced in Drosophila (Hsp70). primary DNA sequence of entire protein-coding region was determined and compared with that Hsp70 Drosophila. two sequences are homologous; could encode a 69,121-Da polypeptide, 48% identical hsp70 protein homology between E. illustrates remarkable conservation shock genes evolution. In contrast Saccharomyces cerevisiae, both which contain multigene families related gene, hybridization analyses...
Protein disulfide bond formation in Escherichia coli requires the periplasmic protein DsbA. We describe here mutations gene for a second protein, DsbB, which is also necessary formation. Evidence suggests that DsbB may act by reoxidizing DsbA, thereby regenerating its ability to donate target proteins. propose an integral membrane be involved transducing redox potential across cytoplasmic membrane.
We have identified promoters for the Escherichia coli heat shock operons dnaK and groE gene encoding protein C62.5. Transcription from each promoter is heat-inducible in vivo, recognized vitro by RNA polymerase containing sigma 32, factor encoded rpoH (htpR) but not 70. compared sequences of propose a consensus sequence, having T-N-t-C-N-C-c-C-T-T-G-A-A -35 region C-C-C-C-A-T-t-T-a -10 region. These differ sequence holoenzyme 70, major E. coli. suggest that accumulated alternate forms are...
ADVERTISEMENT RETURN TO ISSUEPREVArticleNEXTThe reactive and destabilizing disulfide bond of DsbA, a protein required for formation in vivoAndre Zapun, James C. A. Bardwell, Thomas E. CreightonCite this: Biochemistry 1993, 32, 19, 5083–5092Publication Date (Print):May 18, 1993Publication History Published online1 May 2002Published inissue 18 1993https://pubs.acs.org/doi/10.1021/bi00070a016https://doi.org/10.1021/bi00070a016research-articleACS PublicationsRequest reuse permissionsArticle...
DsbA, a thioredoxin superfamily member, introduces disulfide bonds into newly translocated proteins. This process is thought to occur via formation of mixed complexes between DsbA and its substrates. However, these are difficult detect, probably because their short-lived nature. Here we show that it possible detect such covalent intermediates in vivo by mutation alters cis proline-151. Further, this mutant allowed us identify substrates DsbA. Alteration the proline, highly conserved among...
We have isolated a gene from Escherichia coli homologous to the encoding Mr 83,000 Drosophila heat shock protein (hsp83). In E. hsp83 is called C62.5. The predicted amino acid sequence of C62.5 41% and 42% identical human proteins, respectively. Selected regions conservation as high 90%. (named htpG) located between dnaZ adk genes at 11.1 minutes on chromosome. htpG appears be newly identified locus. isolation an homologue illustrates remarkable proteins in evolution will facilitate genetic...
In Escherichia coli, a family of periplasmic disulfide oxidoreductases catalyzes correct bond formation in and secreted proteins. Despite the importance native bonds folding function many proteins, systematic investigation vivo substrates E. coli oxidoreductases, including well characterized oxidase DsbA, has not yet been performed. We combined modified osmotic shock extract two-dimensional gel electrophoresis to identify DsbC, DsbG. found 10 cysteine-containing proteins that are PhoA FlgI,...
Hsp83 is a major eucaryotic heat shock protein and one of the most conserved proteins known. We have isolated an Escherichia coli gene homologous to used it construct deletion mutation. The E. mutant was viable but had slight growth disadvantage that increased with temperature.
The Escherichia coli dnaJ gene product is required for bacteriophage lambda DNA replication at all temperatures. It also essential bacterial viability in least some conditions, since mutations it result temperature-sensitive growth. We have previously cloned the and shown that its migrates as a Mr 37,000 polypeptide under denaturing conditions. Here we present primary sequence of gene. codes processed basic protein (63 51 acidic amino acids) composed 375 acids totaling 40,973. predicted...