Advances in Microbial Physiology, Vol. 54 - download pdf or read online

By Robert K. Poole (Ed.)

ISBN-10: 0123743230

ISBN-13: 9780123743237

Advances in Microbial body structure is among the such a lot profitable and prestigious sequence from educational Press, an imprint of Elsevier. It publishes topical and critical reports, reading body structure to incorporate all fabric that contributes to our realizing of the way microorganisms and their part elements paintings. First released in 1967, it really is now in its fiftieth quantity. The Editors have consistently striven to interpret microbial body structure within the broadest context and feature by no means constrained the contents to "traditional" perspectives of complete cellphone body structure. Now edited by means of Professor Robert Poole, collage of Sheffield, Advances in Microbial body structure is still an influential and extremely good reviewed sequence. * The visit sequence given that 1967 * Contributions by way of major overseas scientists * the newest learn in microbial body structure

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Additional info for Advances in Microbial Physiology, Vol. 54

Sample text

The surface for attachment is shown as a gray box and the polar structures are labeled. Contact with the surface is mediated by flagellar motility, which overcomes repulsive forces (A–B). The flagellum enhances the initial attachment of C. crescentus to the surface (C). Following flagellum ejection, the interaction of the pili with the surface may properly position the cell prior to a more permanent attachment (D). As the swarmer cell differentiates into a stalk cell, the holdfast is exported and the pili are hypothesized to retract (E).

B. BROWN ET AL. , 1993). The exact role of CckA and PleC in mediating stalk biosynthesis is unclear. One possibility is that the stalk defect of CckA and PleC is indirect and related to the role of these proteins in modulating CtrA activity, which is responsible for coupling stalk biogenesis to cell-cycle progression. , 2000, 2002). , 2006b). A phosphorelay cascade involving the hybrid histidine kinase, ShkA, and the Hpt protein, ShpA, mediates the activation of TacA. The signal responsible for initiating the ShkA-ShpATacA phosphorelay remains unknown.

The mechanism of motor control by FliL remains unknown, but recent results suggest that the level of the second messenger, c-di-GMP, may modulate motility and specifically reduce the levels of FliL (Fig. , 2007). Motility is blocked in C. , 2007). , 2007). DgrA is a member of the diguanylate receptor proteins and has a high affinity for binding c-di-GMP. Cells lacking DgrA are motile in the presence of high levels of c-di-GMP and have reduced levels of FliL. However, the levels of other motility proteins including FliM, which is cotranscribed with FliL, are not affected.

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Advances in Microbial Physiology, Vol. 54 by Robert K. Poole (Ed.)


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