We have isolated the Hansenula polymorpha CPY gene encoding carboxypeptidase Y (Hp-CPY). The deduced amino acid sequence revealed that Hp-CPY consists of 541 amino acids and has a calculated Mr of 60,793. The protein is highly similar to Saccharomyces cerevisiae CPY (61β’8% identity). At the N-termin
Cloning and characterization of theHansenula polymorpha homologue of theSaccharomyces cerevisiae PMR1 gene
β Scribed by Kang, Hyun Ah; Kim, Jeong-Yoon; Ko, Su-Min; Park, Cheon Seok; Ryu, Dewey D. Y.; Sohn, Jung-Hoon; Choi, Eui-Sung; Rhee, Sang-Ki
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 228 KB
- Volume
- 14
- Category
- Article
- ISSN
- 0749-503X
No coin nor oath required. For personal study only.
β¦ Synopsis
A gene homologous to Saccharomyces cerevisiae PMR1 has been cloned in the methylotrophic yeast Hansenula polymorpha. The partial DNA fragment of the H. polymorpha homologue was initially obtained by a polymerase chain reaction and used to isolate the entire gene which encodes a protein of 918 amino acids. The putative gene product contains all ten of the conserved regions observed in P-type ATPases. The cloned gene product exhibits 60β’3% amino acid identity to the S. cerevisiae PMR1 gene product and complemented the growth defect of a S. cerevisiae pmr1 null mutant in the EGTA-containing medium. The results demonstrate that the H. polymorpha gene encodes the functional homologue of the S. cerevisiae PMR1 gene product, a P-type Ca 2+ -ATPase. The DNA sequence of the H. polymorpha homologue has been submitted to GenBank with the Accession Number U92083.
π SIMILAR VOLUMES
The squalene synthase (SQS) gene encodes a key regulatory enzyme, farnesyl-diphosphate farnesyltransferase (EC 2.5.1.21), in sterol biosynthesis. The SQS1 gene was isolated from a subgenomic library of the industrially important yeast Yarrowia lipolytica, using PCR-generated probes. Probes were base
The YlEXG1 gene of Yarrowia lipolytica, encoding an exo-1,3--glucanase, was isolated by screening a genomic library with a DNA probe obtained by PCR amplification, using oligonucleotides designed according to conserved regions in the EXG1, EXG2 and SSG1 genes from Saccharomyces cerevisiae. YlEXG1 co
Only a few yeast strains produce pectin-degrading enzymes such as pectin esterases and depolymerases (hydrolases and lyases). Strain SCPP is the only known Saccharomyces strain to produce these pectinases. One of these pectolytic enzymes, PGL1-encoded endopolygalacturonase (EC 3.2.1.15), hydrolyses
Mutations in the Drosophila retinal degeneration B (D-rdgB) gene cause light-enhanced retinal degeneration. Here, we report the isolation of the cDNA encoding human homologue of the D-rdgB and initial characterization of the gene products. Like D-rdgB, the human rdgB homologue (H-rdgB) is a transmem