Read e-book online Advances in Microbial Physiology, Vol. 36 PDF

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

ISBN-10: 0120277360

ISBN-13: 9780120277360

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

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Additional resources for Advances in Microbial Physiology, Vol. 36

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W . SMITH energization being linked to ATP directly. It is to be expected that, at a molecular level, they will resemble model systems in E. coli (Section VI), and we have demonstrated cross-reactivity of antibodies raised against OppA from E. coli with proteins present in shock fluids from Ps. aeruginosa. It is not clear to what extent slow peptide (and amino-acid) transport is a characteristic of the respective permeases, or reflects a ratelimiting penetration of outer membrane porins. A). , 1992).

64). , 1987b). These genes are transcribed in the order opp ABCDF and all are essential for peptide transport controlled by opp. , 1987b). Fusions of LacZ were made to these genes and the hybrid OppB/C-LacZ polypeptides were found to be associated with the cytoplasmic membrane. This location is consistent with the hydrophobicity plots for these proteins, which indicate that each possesses multiple membrane-spanning segments. , 1992). Trypsin accessibility studies helped to identify sections of the polypeptides that were located in the periplasm or cytoplasm.

W . PAYNE A N D M. W. B3). However, in early studies, no dipeptide-binding activity was detected in shock fluids, probably because the affinity of the glycine peptide was too low and it was hydrolysed (Cowell, 1974; results are cited in Payne, 1980b). Studies showing that dipeptide transport was coupled to phosphate-bond energy (arsenate-sensitive) in E. coli supported the idea of a shock-sensitive system (Payne and Bell, 1979; Payne, 1983). Subsequently, this was confirmed when a dipeptide-binding protein (DppA), which was identified from E.

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

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