A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases

Ulla Magdolen; Günter Müller; Viktor Magdolen; Wolfhard Bandlow

doi:10.1016/0167-4781(93)90069-P

A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases

Ulla Magdolen, Günter Müller, Viktor Magdolen, Wolfhard Bandlow

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

32 Scopus citations

Abstract

We have purified bleomycin hydrolase from yeast (molecular mass 55 000 Da). Using protein sequence-derived degenerate oligonucleotide primers and amplification by polymerase chain reaction, the yeast gene BLH1 was isolated and characterized. The deduced amino acid sequence (483 amino acids) exhibits surprisingly high homology to vertebrate bleomycin hydrolase (43% identical residues and 22% conserved exchanges). It contains three blocks of sequences found conserved in other members of the thiol proteinase family and thought to be associated with the catalytic centre. BLH1 is non-essential under all growth conditions tested. However, in the presence of 3.5 mg bleomycin/ml medium wild-type cells have a slight growth advantage compared to blh1 mutant cells.

Original language	English
Pages (from-to)	299-303
Number of pages	5
Journal	Biochimica et Biophysica Acta - Gene Structure and Expression
Volume	1171
Issue number	3
DOIs	https://doi.org/10.1016/0167-4781(93)90069-P
State	Published - 23 Jan 1993
Externally published	Yes

Keywords

(S. cerevisiae)
Antitumor drug
Bleomycin hydrolase gene
Cysteine proteinase

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10.1016/0167-4781(93)90069-P

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title = "A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases",

abstract = "We have purified bleomycin hydrolase from yeast (molecular mass 55 000 Da). Using protein sequence-derived degenerate oligonucleotide primers and amplification by polymerase chain reaction, the yeast gene BLH1 was isolated and characterized. The deduced amino acid sequence (483 amino acids) exhibits surprisingly high homology to vertebrate bleomycin hydrolase (43% identical residues and 22% conserved exchanges). It contains three blocks of sequences found conserved in other members of the thiol proteinase family and thought to be associated with the catalytic centre. BLH1 is non-essential under all growth conditions tested. However, in the presence of 3.5 mg bleomycin/ml medium wild-type cells have a slight growth advantage compared to blh1 mutant cells.",

keywords = "(S. cerevisiae), Antitumor drug, Bleomycin hydrolase gene, Cysteine proteinase",

author = "Ulla Magdolen and G{\"u}nter M{\"u}ller and Viktor Magdolen and Wolfhard Bandlow",

year = "1993",

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doi = "10.1016/0167-4781(93)90069-P",

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volume = "1171",

pages = "299--303",

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publisher = "Elsevier B.V.",

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A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases. / Magdolen, Ulla; Müller, Günter; Magdolen, Viktor et al.
In: Biochimica et Biophysica Acta - Gene Structure and Expression, Vol. 1171, No. 3, 23.01.1993, p. 299-303.

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

TY - JOUR

T1 - A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases

AU - Magdolen, Ulla

AU - Müller, Günter

AU - Magdolen, Viktor

AU - Bandlow, Wolfhard

PY - 1993/1/23

Y1 - 1993/1/23

N2 - We have purified bleomycin hydrolase from yeast (molecular mass 55 000 Da). Using protein sequence-derived degenerate oligonucleotide primers and amplification by polymerase chain reaction, the yeast gene BLH1 was isolated and characterized. The deduced amino acid sequence (483 amino acids) exhibits surprisingly high homology to vertebrate bleomycin hydrolase (43% identical residues and 22% conserved exchanges). It contains three blocks of sequences found conserved in other members of the thiol proteinase family and thought to be associated with the catalytic centre. BLH1 is non-essential under all growth conditions tested. However, in the presence of 3.5 mg bleomycin/ml medium wild-type cells have a slight growth advantage compared to blh1 mutant cells.

AB - We have purified bleomycin hydrolase from yeast (molecular mass 55 000 Da). Using protein sequence-derived degenerate oligonucleotide primers and amplification by polymerase chain reaction, the yeast gene BLH1 was isolated and characterized. The deduced amino acid sequence (483 amino acids) exhibits surprisingly high homology to vertebrate bleomycin hydrolase (43% identical residues and 22% conserved exchanges). It contains three blocks of sequences found conserved in other members of the thiol proteinase family and thought to be associated with the catalytic centre. BLH1 is non-essential under all growth conditions tested. However, in the presence of 3.5 mg bleomycin/ml medium wild-type cells have a slight growth advantage compared to blh1 mutant cells.

KW - (S. cerevisiae)

KW - Antitumor drug

KW - Bleomycin hydrolase gene

KW - Cysteine proteinase

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U2 - 10.1016/0167-4781(93)90069-P

DO - 10.1016/0167-4781(93)90069-P

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AN - SCOPUS:0027394008

SN - 0167-4781

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EP - 303

JO - Biochimica et Biophysica Acta - Gene Structure and Expression

JF - Biochimica et Biophysica Acta - Gene Structure and Expression

IS - 3

ER -

A yeast gene (BLH1) encodes a polypeptide with high homology to vertebrate bleomycin hydrolase, a family member of thiol proteinases

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Keywords

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