Identification and characterization of a novel trans-membrane protein Gene, pdh1, from Schizosaccharomyces pombe

Hidekatsu Iha; Mitsuhiro Takimoto; Inaho Danjoh; Asao Fujiyama

doi:10.1093/dnares/4.6.393

Identification and characterization of a novel trans-membrane protein Gene, pdh1, from Schizosaccharomyces pombe

Hidekatsu Iha, Mitsuhiro Takimoto, Inaho Danjoh, Asao Fujiyama

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

Abstract

We have cloned a new gene, pdh1, from genomic DNA of fission yeast Schizosaccharomyces pombe. pdh1 is actively transcribed as 1400-nucleotide mRNA in vegetatively growing cells and can code for a 226 amino acid polypeptide (pdh1p). Computational structural prediction has revealed that the pdh1p is a highly hydrophobic protein with seven transmembrane domains. The prediction has also detected a possible C-kinase phosphorylation site within the longest hydrophilic loop.

Original language	English
Pages (from-to)	393-396
Number of pages	4
Journal	DNA Research
Volume	4
Issue number	6
DOIs	https://doi.org/10.1093/dnares/4.6.393
Publication status	Published - 1997
Externally published	Yes

Keywords

Fission yeast
Membrane protein
Transmembrane domain

ASJC Scopus subject areas

Molecular Biology
Genetics

Access to Document

10.1093/dnares/4.6.393

Cite this

@article{9594199b50a84c8e85b1fb7fe225aba8,

title = "Identification and characterization of a novel trans-membrane protein Gene, pdh1, from Schizosaccharomyces pombe",

abstract = "We have cloned a new gene, pdh1, from genomic DNA of fission yeast Schizosaccharomyces pombe. pdh1 is actively transcribed as 1400-nucleotide mRNA in vegetatively growing cells and can code for a 226 amino acid polypeptide (pdh1p). Computational structural prediction has revealed that the pdh1p is a highly hydrophobic protein with seven transmembrane domains. The prediction has also detected a possible C-kinase phosphorylation site within the longest hydrophilic loop.",

keywords = "Fission yeast, Membrane protein, Transmembrane domain",

author = "Hidekatsu Iha and Mitsuhiro Takimoto and Inaho Danjoh and Asao Fujiyama",

year = "1997",

doi = "10.1093/dnares/4.6.393",

language = "English",

volume = "4",

pages = "393--396",

journal = "DNA Research",

issn = "1340-2838",

publisher = "Oxford University Press",

number = "6",

}

TY - JOUR

T1 - Identification and characterization of a novel trans-membrane protein Gene, pdh1, from Schizosaccharomyces pombe

AU - Iha, Hidekatsu

AU - Takimoto, Mitsuhiro

AU - Danjoh, Inaho

AU - Fujiyama, Asao

PY - 1997

Y1 - 1997

N2 - We have cloned a new gene, pdh1, from genomic DNA of fission yeast Schizosaccharomyces pombe. pdh1 is actively transcribed as 1400-nucleotide mRNA in vegetatively growing cells and can code for a 226 amino acid polypeptide (pdh1p). Computational structural prediction has revealed that the pdh1p is a highly hydrophobic protein with seven transmembrane domains. The prediction has also detected a possible C-kinase phosphorylation site within the longest hydrophilic loop.

AB - We have cloned a new gene, pdh1, from genomic DNA of fission yeast Schizosaccharomyces pombe. pdh1 is actively transcribed as 1400-nucleotide mRNA in vegetatively growing cells and can code for a 226 amino acid polypeptide (pdh1p). Computational structural prediction has revealed that the pdh1p is a highly hydrophobic protein with seven transmembrane domains. The prediction has also detected a possible C-kinase phosphorylation site within the longest hydrophilic loop.

KW - Fission yeast

KW - Membrane protein

KW - Transmembrane domain

UR - http://www.scopus.com/inward/record.url?scp=0031592991&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0031592991&partnerID=8YFLogxK

U2 - 10.1093/dnares/4.6.393

DO - 10.1093/dnares/4.6.393

M3 - Article

C2 - 9501995

AN - SCOPUS:0031592991

VL - 4

SP - 393

EP - 396

JO - DNA Research

JF - DNA Research

SN - 1340-2838

IS - 6

ER -

Identification and characterization of a novel trans-membrane protein Gene, pdh1, from Schizosaccharomyces pombe

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this