Defect in export and synthesis of the periplasmic galactose receptor MglB in dnaK mutants of Escherichia coli, and decreased stability of the mglB mRNA
Article Abstract:
The high-affinity galactose permease, which comprises the periplasmic galactose receptor MglB, the membrane translocator MglC and the membrane-associated ATPase MglA, exhibited a decreased activity in a dnaK temperature-sensitive mutant of Escherichia coli. This decreased transport activity correlated with a reduction in the quantity of MglB. At 42 degrees Centigrade, there was a reduction in MglB transport. There was also an accumulation of pre-MglB in secB, secA and secY mutants, indicating that SecB and the Sec translocase are also implicated in export of the periplasmic galactose receptor.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1996
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Structural analysis of the 6 kb cryptic plasmid pFAJ2600 from Rhodococcus erythropolis NI86/21 and construction of Escherichia coli - Rhodococcus shuttle vectors
Article Abstract:
A sequence analysis utilizing the bacterial strains and growth conditions of Escherichia coli was conducted to pFAJ26000, a small replicon of a complete nucleotide sequence 5936 bp. Replication of genes in pFAJ2600 showed that deduced proteins RepA and RepB are related to similarly organized genes in a number of cryptic plasmids from various actino-mycetes. The plasmid was also known to carry encoding putative member of the plasmid multimer resolution protein. Furthermore, the sequence analysis of pFAJ2600 showed that some of its regions are unnecessary for stable maintenance in Rhodococcus.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 1997
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Evidence for specific and non-covalent binding of lipids to natural and recombinant Mycobacterium bovis BCG Hsp60 proteins, and to the Escherichia coli homologue GroEL
Article Abstract:
Research has been conducted on the heat-shock proteins from Mycobacterium bovis BCG. Results indicate that lipids are bound non-covalently to heat-shock and homologous proteins.
Publication Name: Microbiology
Subject: Biological sciences
ISSN: 1350-0872
Year: 2000
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