Microbial responses to acidic and alkaline pH are very important in lots of components of bacteriology. for instance, the mechanisms of resistance to acidic pH are vital within the knowing of the passage of human pathogens throughout the acid of the tummy; and an realizing of microbial degradation of alkaline business waste is critical for the environment.
Bringing jointly contributions from a global and interdisciplinary team of specialists engaged on the numerous elements of bacterial mobile responses to pH, this stimulating quantity attracts jointly new and leading edge paintings during this zone. It delineates either similarities and adjustments among mechanisms of tolerance and reaction, offering readers with a useful source at the topic.
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Extra info for Novartis Foundation Symposium 221 - Bacterial Responses to Ph
McLaggan, C. O’Byrne & I. R. Booth, unpublished data 1998). This suggests that the return of pHi to an alkaline value is occasioned by the normal alkalinizing trend of K+ transport activity. Failure of K+ pool regulation may also perturb pH homeostasis. In E. coli cells there is a family of related membrane proteins, the KefA family, that plays a role in osmoregulation. There are five potential members of this family in E. coli and in many organisms there are at least two representatives. The precise role of these systems is far from clear and since they also vary considerably in structural complexity the members may also have evolved separate roles.
Matin: Then why do they stop growing? One can easily engineer conditions in which one can predict why a cell would enter stationary phase, but I don’t see why giving the cells some oxygen would restore pH homeostasis. Stationary phase cells are more resistant to acid stress, but the reason for this is not that they are better at maintaining a pH homeostasis, it’s because of the expression of stress proteins. Slonqewski: The question is, what do people mean when they say ‘stationary phase cells’?
In contrast, the CheZ protein, which facilitates the dephosphorylation of P-CheY, appears to be a special component of the chemotaxis systems of enterics such as E. c d i and Sahzotzer'la. ~ Mechanism of regulation of the kinase CheA CheA is a soluble protein composed of at least four structurally and functionally distinct domains (Fig. 3; Morrison & Parkinson 1994, Stock & Surette 1996). 2 pM (Li et a1 1995, McEvoy et a1 1998, Welch et a1 1998); (iii) the C domain, an approximately 250 amino acid sequence that contains the highly conserved histidine kinase sequence motifs (N-, D-, F- and G-boxes; Stock et a1 1995) and functions to bind ATP and catalyse the phosphorylation of His48; and (iv) the R domain, an approximately 150 amino acid sequence that is required to link CheA to Chew and the receptors.