Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1994-8-5
|
pubmed:databankReference | |
pubmed:abstractText |
Saccharomyces cerevisiae produces two L-asparaginases (ASPs), intracellular ASP I and cell-wall ASP II. In this report, the ASP-I-encoding gene, ASP1, has been identified by homology cloning based on the structures of ASPs from other organisms. Its deduced protein product has a subunit M(r) of 41,414, and shows substantial sequence homology to the bacterial amidohydrolase family. The product of the S. cerevisiae ASP3 gene, a further member of this family, encoding the nitrogen catabolite-regulated cell-wall ASP II, has 46% overall sequence identity to ASP1. Duplication of ancestral asparaginase genes, resulting in separate intra- and extracellular isozymes, appears to have occurred independently in the prokaryotic and eukaryotic lineages. Exact physical mapping of the new cloned ASP1 gene locates it 73% of the distance from the left telomere of chromosome IV, at a position precisely matching the known genetic map location of ASP1. This, along with the structural features of the clone, confirms that ASP1 is the structural gene encoding cytoplasmic ASP I in S. cerevisiae. Sequence analysis of the ethylmethanesulfonate-induced asp1-12 allele of strain XE101-1A revealed a C-->T transition altering Ala176 to Val. This residue lies within a highly conserved region, and the results suggests a critical function for Ala176 in ASP function. Expression of ASP1 and other recombinant ASPs may allow access to improved products for use in the chemotherapy of leukaemia.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Jun
|
pubmed:issn |
0378-1119
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
24
|
pubmed:volume |
144
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
37-43
|
pubmed:dateRevised |
2010-11-18
|
pubmed:meshHeading |
pubmed-meshheading:8026756-Amino Acid Sequence,
pubmed-meshheading:8026756-Asparaginase,
pubmed-meshheading:8026756-Base Sequence,
pubmed-meshheading:8026756-Biological Evolution,
pubmed-meshheading:8026756-Chromosome Mapping,
pubmed-meshheading:8026756-Chromosomes, Fungal,
pubmed-meshheading:8026756-Cloning, Molecular,
pubmed-meshheading:8026756-DNA, Recombinant,
pubmed-meshheading:8026756-Isoenzymes,
pubmed-meshheading:8026756-Molecular Sequence Data,
pubmed-meshheading:8026756-Mutation,
pubmed-meshheading:8026756-Saccharomyces cerevisiae,
pubmed-meshheading:8026756-Sequence Homology, Amino Acid,
pubmed-meshheading:8026756-Transcription, Genetic
|
pubmed:year |
1994
|
pubmed:articleTitle |
The ASP1 gene of Saccharomyces cerevisiae, encoding the intracellular isozyme of L-asparaginase.
|
pubmed:affiliation |
Human Genetics Unit, University of Edinburgh, Western General Hospital, UK.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|