Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803
Autore:
Irmler, A; Forchhammer, K;
Indirizzi:
Univ Giessen, Inst Mikrobiol & Mol Biol, D-35392 Giessen, Germany Univ Giessen Giessen Germany D-35392 Mol Biol, D-35392 Giessen, Germany
Titolo Testata:
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA
fascicolo: 23, volume: 98, anno: 2001,
pagine: 12978 - 12983
SICI:
0027-8424(20011106)98:23<12978:APPDTP>2.0.ZU;2-V
Fonte:
ISI
Lingua:
ENG
Soggetto:
PHOSPHOPROTEIN P-II; GLNB GENE-PRODUCT; SP STRAIN PCC-7942; SYNECHOCOCCUS PCC-7942; GLUTAMINE-SYNTHETASE; TRANSDUCTION; PCC-6803; KINASE; PHOSPHORYLATION; EXPRESSION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
38
Recensione:
Indirizzi per estratti:
Indirizzo: Forchhammer, K Univ Giessen, Inst Mikrobiol & Mol Biol, Heinrich Buff Ring26-32, D-35392Giessen, Germany Univ Giessen Heinrich Buff Ring 26-32 Giessen Germany D-35392
Citazione:
A. Irmler e K. Forchhammer, "A PP2C-type phosphatase dephosphorylates the PII signaling protein in the cyanobacterium Synechocystis PCC 6803", P NAS US, 98(23), 2001, pp. 12978-12983

Abstract

The family of the PH signal transduction proteins contains the most highlyconserved signaling proteins in nature. The cyanobacterial PII-homologue transmits signals of the cellular nitrogen status and carbon status through phosphorylation of a seryl-residue. To identify the enzyme responsible for dephosphorylation of the phosphorylated PH protein in Synechocystis PCC 6803, prospective phosphatase encoding genes were inactivated by targeted insertion of kanamycin resistance cassettes. Disruption of ORF sII1771 generates a mutant unable to dephosphorylate PH under various experimental conditions. On the basis of conserved signature motifs, the sII1771 product (termedPphA) is a member of the protein phosphatase 2C (PP2C) superfamily, which is characterized by Mg2+/Mn2+-dependent catalytic activity. Biochemical analysis of overexpressed and purified PphA confirms its PP2C-type enzymatic properties and demonstrated its reactivity toward the phosphorylated PII protein. Thus, PphA is the first protein phosphatase in Synechocystis PCC 6803for which the physiological substrate and function is known.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 03/12/20 alle ore 05:46:13