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The apyrase KlYnd1p of Kluyveromyces lactis affects glycosylation, secretion, and cell wall properties.

Authors
  • Uccelletti, Daniela
  • Anticoli, Simona
  • Palleschi, Claudio
Type
Published Article
Journal
FEMS yeast research
Publication Date
Aug 01, 2007
Volume
7
Issue
5
Pages
731–739
Identifiers
PMID: 17425676
Source
Medline
License
Unknown

Abstract

The Kluyveromyces lactis ORF r_klactIV3,463 on chromosome IV, hereafter named KlYND1, encodes an endoapyrase that has nucleoside phosphatase activity with a lumenal orientation. The enzyme showed equally high activity towards GDP/UDP and ADP, and also showed activity, although to a lesser extent, towards GTP. No activity was detected with the other triphosphates and all monophosphates. The overexpression of KlYND1 in Klgda1Delta cells of K. lactis, devoid of the encoded GDPase/UDPase activity, suppressed the loss of O-glycosylation and cell wall-related defects described in such mutants, and suggests a partial overlap of function between the two genes, and therefore some redundancy. The overexpression of KlYND1 in wild-type cells enhanced the secretion of the recombinant human serum albumin and glucoamylase employed as reporters.

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