Download Advances in Microbial Physiology, Vol. 36 by A.H. Rose, D.W. Tempest (Ed.) PDF

By A.H. Rose, D.W. Tempest (Ed.)

From the reports of past Volumes "This sequence has continually offered a well-balanced account of development in microbial physiology...Invaluable for educating purposes." -AMERICAN SCIENTIST

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Extra resources for Advances in Microbial Physiology, Vol. 36

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The most important organism involved in peptide breakdown is the Gram-negative Bacteroides ruminicola (Wallace and McKain, 1991). Oligopeptide hydrolysis appears to be initiated mainly through action of an intracellular dipeptidyl aminopeptidase activity. It seems likely from the limited studies described that peptide transport resembles that found for other Gram-negative bacteria. The anaerobe Streptococcus bovis is another important proteolytic bacterium in the rumen, and good evidence for its ability actively to accumulate peptides has been provided (Westlake and Mackie, 1990).

Typhimurium. The nucleotide sequence reported by Abouhamad et al. (1991) was identical to that found by Olson et al. 2 min. Similarities in the sequences of DppA and OppA are also reflected in their structures, for polyclonal antibodies raised against either of the proteins from E. coli cross-react with the other (C. Schuster and J. W. Payne, unpublished results). The protein DppA is amongst the most abundantly produced periplasmic proteins under typical growth conditions, although it is synthesized in smaller amounts than OppA.

1992). The mutants appeared to retain some substrate specificity, implying that the membrane-bound complex possesses some ligand-recognition capacity. The above model for transport is highly speculative and many elements require clarification. Indeed, a fundamental reappraisal of all such models (and see Section XII) may be required following recent evidence on the topography of the membrane complex of the histidine permease of S . , 1993). It appears that the conserved ATPbinding component, HisP, is also exposed to the periplasmic (external) surface, requiring that it be a membrane-spanning protein rather than a peripheral protein confined to the cytoplasmic (inner) surface.

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