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

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

ISBN-10: 0120277360

ISBN-13: 9780120277360

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

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Extra info for Advances in Microbial Physiology, Vol. 36

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B5,6). 5. Regulation of the Dipeptide Permease This aspect has not been studied very intensively, although it is to be expected that it will be subject to similar controls as opp. As a general observation, DppA expression seems somewhat variable amongst different strains of E. coli and S . typhimurium but the reasons for this are obscure. Expression of dpp has been studied in E. coli by monitoring DppA levels under different growth conditions, and in S. typhimurium using dpp-lacZ fusions. In the latter case, production of P-galactosidase (and thus, by presumption, dpp expression) was unaffected by growth in media containing glycerol or glucose, addition of casamino acids or peptides, the level of nitrogenous nutrients or anaerobic growth.

A similar study has been made of the topology of membrane-bound components of the histidine permease; comparisons with similar systems indicated conservation of structural features, and a generalized model for prokaryotic and eukaryotic systems was proposed (Kerppola and Ames, 1992). 24 J W PAYNE AND M. , 1987b). Both are relatively hydrophilic proteins but, despite this, LacZOppD fusion proteins were found to be associated with the cytoplasmic membrane. More precise information on the subcellular location of the OppF protein has come from overproducing the cloned gene product and detecting its presence in cellular fractions using peptidespecific antibodies (Gallagher et al.

18 J . W. PAYNE AND M. W. , 1992). The protein has been purified from S. typhimurium (Hiles and Higgins, 1986) and from E. , 1990). The binding specificities of the protein from E. , 1986). As expected, amino acids showed no competition. The tripeptide Alas was, however, an excellent competitor, although a-Nacetylation abolished its competitive ability and esterification severely decreased it. The specificity towards peptide length was studied using alanine homopeptides. The dipeptide Alaz was not an inhibitor, whereas Ala3 and Ala4 both showed good and similar competitive abilities, while Alas was a relatively poor inhibitor.

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

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