Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha

P. G. Bruinenberg; M. Evers; H. R. Waterham; J. Kuipers; A. C. Arnberg; G. AB

doi:https://doi.org/10.1016/0167-4781(80)90003-2

Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha

P. G. Bruinenberg, M. Evers, H. R. Waterham, J. Kuipers, A. C. Arnberg, G. AB

Other Departments

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

78 Citations (Scopus)

Abstract

We have cloned the AMO gene, encoding the microbody matrix enzyme amine oxidase (EC 1.4.3.6) from the yeast Hansenula polymorpha. The gene was isolated by differential screening of a cDNA library, immunoselection, and subsequent screening of a H. polymorpha genomic library. The nucleotide sequence of a 3.6 kilobase stretch of DNA containing the amine oxidase (AMO) gene was determined. The AMO gene contains an open reading frame of 692 amino acids, with a relative molecular mass of 77,435. The 5' and 3' ends of the gene were mapped and show that the transcribed region measures 2134 nucleotides. The derived amino-acid sequence was confirmed by sequencing an internal proteolytic fragment of the purified protein. Amine oxidase contains the tripeptide sequence Ser-Arg-Leu, located 9 residues from the carboxy terminus, which may represent the topogenic signal for protein import into microbodies

Original language	English
Pages (from-to)	157-167
Journal	BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION
Volume	1008
Issue number	2
DOIs	https://doi.org/10.1016/0167-4781(80)90003-2
Publication status	Published - 1989

Access to Document

https://doi.org/10.1016/0167-4781(80)90003-2

Cite this

@article{92a115de56d242ca855e79528afd79fe,

title = "Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha",

abstract = "We have cloned the AMO gene, encoding the microbody matrix enzyme amine oxidase (EC 1.4.3.6) from the yeast Hansenula polymorpha. The gene was isolated by differential screening of a cDNA library, immunoselection, and subsequent screening of a H. polymorpha genomic library. The nucleotide sequence of a 3.6 kilobase stretch of DNA containing the amine oxidase (AMO) gene was determined. The AMO gene contains an open reading frame of 692 amino acids, with a relative molecular mass of 77,435. The 5' and 3' ends of the gene were mapped and show that the transcribed region measures 2134 nucleotides. The derived amino-acid sequence was confirmed by sequencing an internal proteolytic fragment of the purified protein. Amine oxidase contains the tripeptide sequence Ser-Arg-Leu, located 9 residues from the carboxy terminus, which may represent the topogenic signal for protein import into microbodies",

author = "Bruinenberg, {P. G.} and M. Evers and Waterham, {H. R.} and J. Kuipers and Arnberg, {A. C.} and G. AB",

year = "1989",

doi = "https://doi.org/10.1016/0167-4781(80)90003-2",

language = "English",

volume = "1008",

pages = "157--167",

journal = "BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION",

issn = "0167-4781",

publisher = "Elsevier BV",

number = "2",

}

TY - JOUR

T1 - Cloning and sequencing of the peroxisomal amine oxidase gene from Hansenula polymorpha

AU - Bruinenberg, P. G.

AU - Evers, M.

AU - Waterham, H. R.

AU - Kuipers, J.

AU - Arnberg, A. C.

AU - AB, G.

PY - 1989

Y1 - 1989

N2 - We have cloned the AMO gene, encoding the microbody matrix enzyme amine oxidase (EC 1.4.3.6) from the yeast Hansenula polymorpha. The gene was isolated by differential screening of a cDNA library, immunoselection, and subsequent screening of a H. polymorpha genomic library. The nucleotide sequence of a 3.6 kilobase stretch of DNA containing the amine oxidase (AMO) gene was determined. The AMO gene contains an open reading frame of 692 amino acids, with a relative molecular mass of 77,435. The 5' and 3' ends of the gene were mapped and show that the transcribed region measures 2134 nucleotides. The derived amino-acid sequence was confirmed by sequencing an internal proteolytic fragment of the purified protein. Amine oxidase contains the tripeptide sequence Ser-Arg-Leu, located 9 residues from the carboxy terminus, which may represent the topogenic signal for protein import into microbodies

AB - We have cloned the AMO gene, encoding the microbody matrix enzyme amine oxidase (EC 1.4.3.6) from the yeast Hansenula polymorpha. The gene was isolated by differential screening of a cDNA library, immunoselection, and subsequent screening of a H. polymorpha genomic library. The nucleotide sequence of a 3.6 kilobase stretch of DNA containing the amine oxidase (AMO) gene was determined. The AMO gene contains an open reading frame of 692 amino acids, with a relative molecular mass of 77,435. The 5' and 3' ends of the gene were mapped and show that the transcribed region measures 2134 nucleotides. The derived amino-acid sequence was confirmed by sequencing an internal proteolytic fragment of the purified protein. Amine oxidase contains the tripeptide sequence Ser-Arg-Leu, located 9 residues from the carboxy terminus, which may represent the topogenic signal for protein import into microbodies

U2 - https://doi.org/10.1016/0167-4781(80)90003-2

DO - https://doi.org/10.1016/0167-4781(80)90003-2

M3 - Article

C2 - 2500147

SN - 0167-4781

VL - 1008

SP - 157

EP - 167

JO - BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION

JF - BIOCHIMICA ET BIOPHYSICA ACTA-GENE STRUCTURE AND EXPRESSION

IS - 2

ER -