pzl-1 encodes a novel protein phosphatase-Z-like Ser/Thr protein phosphatase in Neurospora crassa

Balázs Szöor; Zsigmond Fehér; Tamás Zeke; Pál Gergely; Einat Yatzkan; Oded Yarden; Viktor Dombrádi

doi:10.1016/S0167-4838(98)00201-5

pzl-1 encodes a novel protein phosphatase-Z-like Ser/Thr protein phosphatase in Neurospora crassa

Balázs Szöor, Zsigmond Fehér, Tamás Zeke, Pál Gergely, Einat Yatzkan, Oded Yarden, Viktor Dombrádi^*

^*Corresponding author for this work

Department of Plant Pathology and Microbiology

Research output: Contribution to journal › Article › peer-review

10 Scopus citations

Abstract

The gene and cDNA of a novel protein phosphatase were cloned from Neurospora crassa. The pzl-1 gene encompasses three introns and is localized to the left arm of chromosome I between cyt-21 and Fsr-12. It encodes a protein of 58.3 kDa containing a Ser/Pro rich N-terminal segment, and a C-terminal domain that is similar to the catalytic subunit of type 1 protein phosphatases. The first 51 amino acid residues, including a potential N-myristoylation site, as well as the C-terminal domain (about 300 residues) have a high level of sequence identity with yeast PPZ phosphatases. However, residues 52-208 do not share high similarity with other proteins. The mRNA of pzl-1 was detected in all phases of asexual development of the filamentous fungus. Copyright (C) 1998 Elsevier Science B.V.

Original language	English
Pages (from-to)	260-266
Number of pages	7
Journal	Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology
Volume	1388
Issue number	1
DOIs	https://doi.org/10.1016/S0167-4838(98)00201-5
State	Published - 14 Oct 1998

Bibliographical note

Funding Information:
This work was supported by the Hungarian Research Council, Grant OTKA 22675, BARD – The US/Israel Binational Agricultural Research and Development Fund, and a bilateral Israeli/Hungarian exchange program ISR-2/96. B.S. was the recipient of a CEF 1559 travel fellowship. The authors thank Dr. Joaquin Ariño and Dr. János Pósfai for their valuable comments on the sequences.

Keywords

Fungal development
Neurospora crassa
PPZ-like protein
Ser/Thr protein phosphatase

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abstract = "The gene and cDNA of a novel protein phosphatase were cloned from Neurospora crassa. The pzl-1 gene encompasses three introns and is localized to the left arm of chromosome I between cyt-21 and Fsr-12. It encodes a protein of 58.3 kDa containing a Ser/Pro rich N-terminal segment, and a C-terminal domain that is similar to the catalytic subunit of type 1 protein phosphatases. The first 51 amino acid residues, including a potential N-myristoylation site, as well as the C-terminal domain (about 300 residues) have a high level of sequence identity with yeast PPZ phosphatases. However, residues 52-208 do not share high similarity with other proteins. The mRNA of pzl-1 was detected in all phases of asexual development of the filamentous fungus. Copyright (C) 1998 Elsevier Science B.V.",

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author = "Bal{\'a}zs Sz{\"o}or and Zsigmond Feh{\'e}r and Tam{\'a}s Zeke and P{\'a}l Gergely and Einat Yatzkan and Oded Yarden and Viktor Dombr{\'a}di",

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AU - Yatzkan, Einat

AU - Yarden, Oded

AU - Dombrádi, Viktor

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AB - The gene and cDNA of a novel protein phosphatase were cloned from Neurospora crassa. The pzl-1 gene encompasses three introns and is localized to the left arm of chromosome I between cyt-21 and Fsr-12. It encodes a protein of 58.3 kDa containing a Ser/Pro rich N-terminal segment, and a C-terminal domain that is similar to the catalytic subunit of type 1 protein phosphatases. The first 51 amino acid residues, including a potential N-myristoylation site, as well as the C-terminal domain (about 300 residues) have a high level of sequence identity with yeast PPZ phosphatases. However, residues 52-208 do not share high similarity with other proteins. The mRNA of pzl-1 was detected in all phases of asexual development of the filamentous fungus. Copyright (C) 1998 Elsevier Science B.V.

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pzl-1 encodes a novel protein phosphatase-Z-like Ser/Thr protein phosphatase in Neurospora crassa

Abstract

Bibliographical note

Keywords

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