Cloning and characterization of the Aspergillus nidulans cysB gene encoding cysteine synthase

The cysB gene of A. nidulans was cloned by complementation of a cysB mutation. This is the first cloned eukaryotic genomic sequence coding for cysteine synthase. The gene contains one 71-bp intron and codes for a protein of 370 amino acids. Its N-terminal region has characteristic features of transi...

Full description

Saved in:
Bibliographic Details
Published in:Current genetics 1997-04, Vol.31 (4), p.348-356
Main Authors: Topczewski, J, Sienko, M, Paszewski, A
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Amino Acids, Sulfur - genetics
Amino Acids, Sulfur - metabolism
ASPERGILLUS NIDULANS
Aspergillus nidulans - genetics
Aspergillus nidulans - metabolism
Base Sequence
CISTEINA
CLONACION MOLECULAR
CLONAGE MOLECULAIRE
Cloning, Molecular
CYSB
CYSTEINE
CYSTEINE SYNTHASE
Cysteine Synthase - genetics
Cysteine Synthase - metabolism
DNA, Complementary - genetics
EC 4.2.99.8
GENE
GENES
LIGASAS
LIGASE
LIGASES
Mitochondria - chemistry
Mitochondria - metabolism
MOLECULAR CLONING
Molecular Sequence Data
NUCLEOTIDE SEQUENCE
Phylogeny
Restriction Mapping
RNA, Messenger - genetics
SECUENCIA NUCLEOTIDICA
Sequence Analysis, DNA
Sequence Homology, Amino Acid
SEQUENCE NUCLEOTIDIQUE
Citations: Items that cite this one
Online Access:Get full text
Tags: Add Tag
No Tags, Be the first to tag this record!
Description
Summary:The cysB gene of A. nidulans was cloned by complementation of a cysB mutation. This is the first cloned eukaryotic genomic sequence coding for cysteine synthase. The gene contains one 71-bp intron and codes for a protein of 370 amino acids. Its N-terminal region has characteristic features of transit peptides, suggesting mitochondrial localisation of the enzyme. The protein shows homology with bacterial and plant cysteine synthases among which it occupies a remote phylogenetic position and apparently represents a distinct subfamily. Transcription of the cysB gene is not appreciably regulated by the concentration of methionine in the growth medium.
ISSN:0172-8083
1432-0983
DOI:10.1007/s002940050215