Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
Isolation and characterization of par1+ and par2+: Two Schizosaccharomycespombe genes encoding B ' subunits of protein phosphatase 2A
Autore:
Jiang, W; Hallberg, RL;
Indirizzi:
Syracuse Univ, Dept Biol, Syracuse, NY 13244 USA Syracuse Univ Syracuse NY USA 13244 iv, Dept Biol, Syracuse, NY 13244 USA
Titolo Testata:
GENETICS
fascicolo: 3, volume: 154, anno: 2000,
pagine: 1025 - 1038
SICI:
0016-6731(200003)154:3<1025:IACOPA>2.0.ZU;2-P
Fonte:
ISI
Lingua:
ENG
Soggetto:
SERINE THREONINE PHOSPHATASES; FISSION YEAST; REGULATORY SUBUNIT; SACCHAROMYCES-CEREVISIAE; SEPTUM FORMATION; SERINE/THREONINE PHOSPHATASES; CELL-GROWTH; A-SUBUNIT; CYTOKINESIS; IDENTIFICATION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Agriculture,Biology & Environmental Sciences
Life Sciences
Citazioni:
53
Recensione:
Indirizzi per estratti:
Indirizzo: Hallberg, RL Syracuse Univ, Dept Biol, 411 Lyman Hall,108 Coll Pl, Syracuse, NY 13244 USA Syracuse Univ 411 Lyman Hall,108 Coll Pl Syracuse NY USA 13244
Citazione:
W. Jiang e R.L. Hallberg, "Isolation and characterization of par1+ and par2+: Two Schizosaccharomycespombe genes encoding B ' subunits of protein phosphatase 2A", GENETICS, 154(3), 2000, pp. 1025-1038

Abstract

Protein phosphatase 2A (PP2A) is one of the major scrine/threonine phosphatases found in eukaryotic cells. We cloned two genes, par1(+) and par2(+), encoding distinct B' subunits of PP2A in fission yeast. They share 52% identity at the amino acid sequence level. Neither gene is essential but together they are required for normal septum positioning and cytokineses, for growth at both high and low temperature, and for growth under a number of stressful conditions. Immunofluorescence microscopy revealed that Par2p has a cell-cycle-related localization pattern, being localized at cell ends duringinterphase and forming a medial ring in cells that are undergoing septation and cytokinesis. Our analyses also indicate that Par1p is more abundant than Par2p in the cell. Cross-organism studies showed. that both par1(+) andpar2(+) could complement the rts1 Delta allele in Saccharomyces cervisiae,albeit to different extents, in spite of the fact that neither contains a serine/threonine-rich N-terminal domain like th;lr round in the S. cerevisiae homolog Rrs1p. Thus, while Schizosaccharomyces pombe is more similar to higher eukaryotes with respect to its complement of B'-encoding genes, the function of those proteins is conserved relative to that of Rts1p.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 20/01/20 alle ore 21:57:29