Open AccessThe apyrase KlYnd1p of Kluyveromyces lactis affects glycosylation, secretion, and cell wall properties
Author(s) -
Uccelletti Daniela,
Anticoli Simona,
Palleschi Claudio
Publication year - 2007
Publication title -
fems yeast research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.991
H-Index - 92
eISSN - 1567-1364
pISSN - 1567-1356
DOI - 10.1111/j.1567-1364.2007.00229.x
Subject(s) - kluyveromyces lactis , biology , kluyveromyces , biochemistry , secretion , glycosylation , phosphatase , apyrase , gene , enzyme , microbiology and biotechnology , saccharomyces cerevisiae
The Kluyveromyces lactis ORF r_klactIV3463 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 Klgda1 Δ 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.