Current Topics in Microbiology and Immunology 129 by J. M. Brass (auth.), A. Clarke, R. W. Compans, M. Cooper, H.

By J. M. Brass (auth.), A. Clarke, R. W. Compans, M. Cooper, H. Eisen, W. Goebel, H. Koprowski, F. Melchers, M. Oldstone, R. Rott, P. K. Vogt, H. Wagner, I. Wilson (eds.)

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1986), the cell division machinery must provide mechanisms to: (a) identify the mid-point of the cell; (b) initiate the changes in molecular organization that commit this site to the division process; (c) facilitate the invagination of inner membrane, murein, and outer membrane and the subsequent separation of the daughter cells; and (d) ensure that each progeny cell receives at least one copy of the bacterial chromosome during this process. Evidence has been presented that extended zones of attachment between murein and the inner and outer membranes playa role in one or more of these aspects of the division process.

In addition, CAP sites are indicated; that of malPp is dispensible. Numbers indicate the distance (nucleotides) between the sequences; small letters, nucleotides completely conserved in all MalT binding sites; stars, nucleotides whose alteration decreases promoter activity; numbers above, positions of nucleotides with respect to the transcription startpoint in malPp ' (Modified from RAlBAUD et aL 1985) and adenylate cyclase, respectively, are unable to grow on maltose (SCHWARTZ and BECKWITH 1970; PERLMAN and PASTAN 1969).

In most cases a similar Km of the respective transport system is found. All binding protein tested so far showed a pronounced conformational change upon binding of substrate, which could be assayed as a change in the fluorescence spectrum, or by other techniques. Three sugar binding proteins (galactose- ribose-, and maltose-binding proteins) and probably a dipeptide-binding protein, but none of the numerous other binding proteins, function as chemoreceptors in chemotaxis (see Chap. 9). All periplasmic proteins, including the binding proteins, are synthesized as precursors on membrane-bound ribosomes.

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