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Titolo:
Precise amounts of a novel member of a phosphotransferase superfamily are essential for growth and normal morphology in Caulobacter crescentus
Autore:
Fuchs, T; Wiget, P; Osteras, M; Jenal, U;
Indirizzi:
Univ Basel, Biozentrum, Div Mol Microbiol, CH-4056 Basel, Switzerland UnivBasel Basel Switzerland CH-4056 crobiol, CH-4056 Basel, Switzerland
Titolo Testata:
MOLECULAR MICROBIOLOGY
fascicolo: 3, volume: 39, anno: 2001,
pagine: 679 - 692
SICI:
0950-382X(200102)39:3<679:PAOANM>2.0.ZU;2-7
Fonte:
ISI
Lingua:
ENG
Soggetto:
RESPONSE REGULATOR PROTEIN; ESCHERICHIA-COLI K-12; P-TYPE ATPASE; GENETIC-ANALYSIS; CELL-SHAPE; RODA GENE; IDENTIFICATION; DEHALOGENASE; MUTAGENESIS; SITE;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
48
Recensione:
Indirizzi per estratti:
Indirizzo: Jenal, U Univ Basel, Biozentrum, Div Mol Microbiol, CH-4056 Basel, Switzerland Univ Basel Basel Switzerland CH-4056 CH-4056 Basel, Switzerland
Citazione:
T. Fuchs et al., "Precise amounts of a novel member of a phosphotransferase superfamily are essential for growth and normal morphology in Caulobacter crescentus", MOL MICROB, 39(3), 2001, pp. 679-692

Abstract

The Caulobacter crescentus chromosomal clp locus contains the genes encoding the components of ClpXP, a multisubunit protease required for cell cycleprogression in this organism. Here, we report the identification and characterization of cicA, a gene located between the clpX and clpP genes on the Caulobacter chromosome. cicA is a novel morphogene in C. crescentus and, like clpX and clpP, is essential for growth. A conditional cicA mutant stopped growth, but retained viability under restrictive conditions. In contrast,an increased concentration of CicA led to an immediate loss of the normal rod shape, an almost 10-fold increase of the cell's volume and a cell division block. In parallel with this drastic morphological change, cells rapidly lost viability. Primary sequence analysis suggested that the cicA gene encodes a member of a large superfamily of phosphotransferases, that include phosphoserine phosphatases, the ATPase domain of P-type ATPases and receiver domains of response regulators. Four conserved motifs of this protein family that have been implicated in the catalysis of phosphotransfer reactionswere investigated by site-directed mutagenesis and were found to be critical for in vivo function of CicA, Based on our observations, we postulate that CicA is involved in essential phosphotransferase reactions in Caulobacter and that increased activity of CicA has a deleterious effect on cell wallbiosynthesis, morphogenesis and cell division.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 15/01/21 alle ore 21:59:00