Molecular characterization of protein O-mannosyltransferase and its involvement in cell-wall synthesis in Aspergillus nidulans.

نویسندگان

  • Takuji Oka
  • Tetsu Hamaguchi
  • Yuka Sameshima
  • Masatoshi Goto
  • Kensuke Furukawa
چکیده

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 pmtA gene resulted in the reduction of in vitro protein O-d-mannosyltransferase activity to 6 % of that of the wild-type strain and led to underglycosylation of an extracellular glucoamylase. The pmtA disruptant exhibited abnormal cell morphology and alteration in carbohydrate composition, particularly reduction in the skeletal polysaccharides in the cell wall. The results indicate that PmtA is required for the formation of a normal cell wall in A. nidulans.

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

منابع مشابه

Reduced expression of the O-mannosyltransferase 2 (AfPmt2) leads to deficient cell wall and abnormal polarity in Aspergillus fumigatus.

Protein O-mannosyltransferases (PMTs) initiate O-mannosylation of secretory proteins, which are of fundamental importance in eukaryotes. The human fungal pathogen Aspergillus fumigatus possesses three genes encoding for PMTs, namely, Afpmt1, Afpmt2 and Afpmt4. We have previously shown that lack of AfPmt1 leads to a temperature-sensitive phenotype featured with severe defects in hyphal growth, c...

متن کامل

O-Mannosyltransferase 1 in Aspergillus fumigatus (AfPmt1p) is crucial for cell wall integrity and conidium morphology, especially at an elevated temperature.

Protein O-mannosyltransferases initiate O mannosylation of secretory proteins, which are of fundamental importance in eukaryotes. In this study, the PMT gene family of the human fungal pathogen Aspergillus fumigatus was identified and characterized. Unlike the case in Saccharomyces cerevisiae, where the PMT family is highly redundant, only one member of each PMT subfamily, namely, Afpmt1, Afpmt...

متن کامل

Plant Defensins NaD1 and NaD2 Induce Different Stress Response Pathways in Fungi

Nicotiana alata defensins 1 and 2 (NaD1 and NaD2) are plant defensins from the ornamental tobacco that have antifungal activity against a variety of fungal pathogens. Some plant defensins interact with fungal cell wall O-glycosylated proteins. Therefore, we investigated if this was the case for NaD1 and NaD2, by assessing the sensitivity of the three Aspergillus nidulans (An) O-mannosyltransfer...

متن کامل

CsmA, a class V chitin synthase with a myosin motor-like domain, is localized through direct interaction with the actin cytoskeleton in Aspergillus nidulans.

One of the essential features of fungal morphogenesis is the polarized synthesis of cell wall components such as chitin. The actin cytoskeleton provides the structural basis for cell polarity in Aspergillus nidulans, as well as in most other eukaryotes. A class V chitin synthase, CsmA, which contains a myosin motor-like domain (MMD), is conserved among most filamentous fungi. The DeltacsmA null...

متن کامل

Aspergillus nidulans Cell Wall Composition and Function Change in Response to Hosting Several Aspergillus fumigatus UDP-Galactopyranose Mutase Activity Mutants

Deletion or repression of Aspergillus nidulans ugmA (AnugmA), involved in galactofuranose biosynthesis, impairs growth and increases sensitivity to Caspofungin, a β-1,3-glucan synthesis antagonist. The A. fumigatus UgmA (AfUgmA) crystal structure has been determined. From that study, AfUgmA mutants with altered enzyme activity were transformed into AnugmA▵ to assess their effect on growth and w...

متن کامل

ذخیره در منابع من


  با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید

برای دانلود متن کامل این مقاله و بیش از 32 میلیون مقاله دیگر ابتدا ثبت نام کنید

ثبت نام

اگر عضو سایت هستید لطفا وارد حساب کاربری خود شوید

عنوان ژورنال:
  • Microbiology

دوره 150 Pt 6  شماره 

صفحات  -

تاریخ انتشار 2004