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Elongation bacterial

MCPs or MCP-like receptors appear to be involved in most, if not all, chemotactically responsive bacterial species (e.g., [410]). In all bacterial and archaeal species examined, the MCPs are clustered at the poles. In elongated bacterial species, the MCPs are located both at the poles and at regions along the length of the cells [257]. The number of MCPs varies a lot between species, from 5 in E. coli to 43 in Vibrio cholerae [288], which is the current record-holder. While the MCPs of many species are similar to those of E. coli and Salmonella, others are significantly different. A few examples follow. [Pg.122]

When bacteria multiply through cell division, FtsZ is the first protein recruited to the division site and thereby defines the geometry of binary fission. Moreover, it directs the production of a new cell wall between the separating parts of the cell and is thus absolutely essential to bacterial reproduction. A temperature-sensitive mutant strain devoid of FtsZ above a certain temperature showed a filamenta-tion phenotype exactly as observed with ADEP-treated cells. In summary, ADEP-overactivated CIpP degrades FtsZ, which prevents cell division, causes the formation of massively elongated bacterial cells, and ultimately leads to cell death [7]. [Pg.215]

So this research reveals new mechanisms of bacterial autoregulation under extreme conditions, controlled by low weight molecules - alkyiresorcinols. It applied aspects are defined by developing of methods for DNA protection in vitro and elongators of bacterial cells viability at UV exposure. [Pg.197]

Bacterial ribosome function Aminoglycosides Tetracyclines Chloramphenicol Macrolides, azalides Fusidic acid Mupirocin Distort SOS ribosomal subunit Block SOS ribosomal subunit Inhibits peptidyl transferase Block translocation Inhibits elongation factor Inhibits isoleucyl-tRNA synthesis No action on 40S subunit Excluded by mammalian cells No action on mammalian equivalent No action on mammalian equivalent Excluded by mammalian cells No action on mammalian equivalent... [Pg.163]

J. E. Loper and M. N. Schroth, Influence of bacterial sources of indole-3-acetic acid on root elongation of sugar beet. Phytopathology 76 386 (1986). [Pg.135]

A. Caused bacterial death B. Caused no change C. Caused elongation... [Pg.7]

A third type of bacterial toxin, diphtheria toxin, catalyzes the ADP-ribosylation of eukaryotic elongation factor (EFTU), a type of small G protein involved in protein synthesis (Table 19-2). The functional activity of the elongation factor is inhibitedby this reaction. Finally, a botulinum toxin ADP-ribosylates and disrupts the function of the small G protein Rho, which appears to be involved in assembly and rearrangement of the actin cytoskeleton (Table 19-2). These toxins maybe involved in neuropathy (see Ch. 36) and membrane trafficking (see Ch. 9). [Pg.344]

Coccobacillus A short, thick bacterial rod of the shape of an oval or slightly elongated coccus. [Pg.303]

Based on the same principle, there are monomeric / -helical proteins that carry at their extremities a cluster of helical or nonrepetitive structures that could act as a capping element covering their exposed ends (Emsley et al., 1996 Lietzke et al, 1994 Petersen et al, 1997 Steinbacher et al, 1994). For example, the last 40 residues of pectate lyase C form a large loop that partially covers the surface of the /Hielix (Yoder et al, 1993). The fibrous (or otherwise elongated) domain of these natural /f-stranded proteins is not stable in isolation, as for example in the case of the P22 tailspike where bacterially expressed isolated /Hielix domain, at high concentrations, forms fibrous aggregates that bind Congo red (Schuler et al, 1999). [Pg.113]

In eukaryotic cells, the number of initiation factors is larger and initiation is therefore more complex than in prokaryotes. The cap at the 5 end of mRNA and the polyA tail (see p. 246) play important parts in initiation. However, the elongation and termination processes are similar in all organisms. The individual steps of bacterial translation can be inhibited by antibiotics (see p. 254). [Pg.252]

This bacterial ADPRtransferase inactivates host cell ri-bosomal elongation factor eEF-2 by NAD+-dependent covalent modification of diphthamide, an acceptor-modified histidyl residue, 2-[3-carboxyamido-3-(trimethylam-monio)propyl]histidine. [Pg.204]


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See also in sourсe #XX -- [ Pg.55 , Pg.56 ]

See also in sourсe #XX -- [ Pg.55 , Pg.56 ]




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Elongation of bacterial DNA

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