Source:http://linkedlifedata.com/resource/pubmed/id/11169754
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
2
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pubmed:dateCreated |
2001-2-22
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pubmed:abstractText |
The gene pzl-1 from the filamentous fungus Neurospora crassa encodes a putative Ser/Thr protein phosphatase that is reminiscent of the Ppz1/Ppz2 and Pzh1 phosphatases from Saccharomyces cerevisiae and Schizosaccharomyces pombe, respectively. The entire PZL-1 protein, as well as its carboxyl-terminal domain, have been expressed in Escherichia coli as active protein phosphatases. To characterize its cellular role, PZL-1 was also expressed in Sz. pombe and in S. cerevisiae. Expression of PZL-1 in S. cerevisiae from the PPZ1 promoter was able to rescue the altered sensitivity to caffeine and lithium ions of a ppz1 strain. Furthermore, high copy number expression of PZL-1 alleviated the lytic phenotype of a S. cerevisiae slt2/mpk1 mitogen-activated protein (MAP) kinase mutant, similarly to that described for PPZ1, and mimicked the effects of high levels of Ppz1 on cell growth. Expression of PZL-1 in fission yeast from a weak version of the nmt1 promoter fully rescued the growth defect of a pzh1Delta strain in high potassium, but only partially complemented the sodium-hypertolerant phenotype. Strong overexpression of the N. crassa phosphatase in Sz. pombe affected cell growth and morphology. Therefore, PZL-1 appears to fulfil every known function carried out by its S. cerevisiae counterpart, despite the marked divergence in sequence within their NH(2)-terminal moieties.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Fungal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/PPZ1 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/SIS2 protein, S cerevisiae,
http://linkedlifedata.com/resource/pubmed/chemical/Saccharomyces cerevisiae Proteins
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pubmed:status |
MEDLINE
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pubmed:month |
Jan
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pubmed:issn |
0749-503X
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pubmed:author | |
pubmed:copyrightInfo |
Copyright 2000 John Wiley & Sons, Ltd.
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pubmed:issnType |
Print
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pubmed:day |
30
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pubmed:volume |
18
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
115-24
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:11169754-Catalytic Domain,
pubmed-meshheading:11169754-Cell Cycle,
pubmed-meshheading:11169754-Cell Cycle Proteins,
pubmed-meshheading:11169754-Cloning, Molecular,
pubmed-meshheading:11169754-Escherichia coli,
pubmed-meshheading:11169754-Fungal Proteins,
pubmed-meshheading:11169754-Gene Expression,
pubmed-meshheading:11169754-Neurospora crassa,
pubmed-meshheading:11169754-Phosphoprotein Phosphatases,
pubmed-meshheading:11169754-Saccharomyces cerevisiae,
pubmed-meshheading:11169754-Saccharomyces cerevisiae Proteins,
pubmed-meshheading:11169754-Schizosaccharomyces
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pubmed:year |
2001
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pubmed:articleTitle |
Functional analysis of the Neurospora crassa PZL-1 protein phosphatase by expression in budding and fission yeast.
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pubmed:affiliation |
Department of Medical Chemistry, Faculty of Medicine, Medical and Health Science Centre, University of Debrecen, H-4026 Debrecen, Hungary.
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pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
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