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Functional analysis of the Neurospora crassa PZL‐1 protein phosphatase by expression in budding and fission yeast
Author(s) -
Vissi Emese,
Clotet Josep,
de Nadal Eulalia,
Barceló Anna,
Bakó Éva,
Gergely Pál,
Dombrádi Viktor,
Ariño Joaquín
Publication year - 2001
Publication title -
yeast
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.923
H-Index - 102
eISSN - 1097-0061
pISSN - 0749-503X
DOI - 10.1002/1097-0061(20010130)18:2<115::aid-yea653>3.0.co;2-g
Subject(s) - neurospora crassa , schizosaccharomyces pombe , biology , saccharomyces cerevisiae , phosphatase , schizosaccharomyces , fungal protein , protein phosphatase 2 , protein kinase a , crassa , mutant , yeast , microbiology and biotechnology , kinase , biochemistry , gene , enzyme
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 pzh1 Δ 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. Copyright © 2000 John Wiley & Sons, Ltd.