Protein O-mannosyltransferase A of Aspergillus awamori is involved in O-mannosylation of glucoamylase I
نویسندگان
چکیده
منابع مشابه
O-glycosylation in Aspergillus glucoamylase. Conformation and role in binding.
Functional peptides have been produced by proteolysis of glucoamylase (glucan 1,4-alpha-glucosidase; EC 3.2.1.3) from Aspergillus niger and purified by affinity chromatography, gel filtration and two ion-exchange-chromatography steps. The peptides correspond to residues 499-616 and 509-616 of the original glucoamylase molecule. Together with G1C (residues 471-616 from glucoamylase 1) [Belshaw &...
متن کاملO-mannosylation of cadherins.
Two reports in PNAS by Vester-Christensen et al. (1) and Lommel et al. (2) provide critical new insight into how a unique family of glycans contributes to early embryonic development, brain development, and malignant transformation. Following transfer of mannose (Man) to Ser or Thr by protein Omannosyltransferase (POMT), either POMT1 or POMT2, the O-Man can be further modified with N-acetylgluc...
متن کاملMolecular characterization of protein O-mannosyltransferase and its involvement in cell-wall synthesis in Aspergillus nidulans.
Protein O-glycosylation is essential for protein modification and plays important roles in eukaryotic cells. O-Mannosylation of proteins occurs in the filamentous fungus Aspergillus. The structure and function of the pmtA gene, encoding protein O-d-mannosyltransferase, which is responsible for the initial O-mannosylation reaction in Aspergillus nidulans, was characterized. Disruption of the pmt...
متن کاملDom34 Links Translation to Protein O-mannosylation
In eukaryotes, Dom34 upregulates translation by securing levels of activatable ribosomal subunits. We found that in the yeast Saccharomyces cerevisiae and the human fungal pathogen Candida albicans, Dom34 interacts genetically with Pmt1, a major isoform of protein O-mannosyltransferase. In C. albicans, lack of Dom34 exacerbated defective phenotypes of pmt1 mutants, while they were ameliorated b...
متن کاملProtein engineering of Aspergillus awamori glucoamylase to increase its pH optimum.
To increase the pH optimum of glucoamylase (GA), five mutations-S411G, S411A, S411C, S411H and S411D--were designed to destabilize the carboxylate ion form of Glu400, the catalytic base, by removing or weakening the hydrogen bond between Ser411 and Glu400, and thereby raising its pK. The substitution of alanine, histidine and aspartate were also designed to study the additional effects of polar...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Microbiology
سال: 2005
ISSN: 1350-0872,1465-2080
DOI: 10.1099/mic.0.28088-0