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PYP-1, inorganic pyrophosphatase, is required for larval development and intestinal function in C-elegansopen access

Authors
Ko, Kyung MinLee, WonhaeYu, Jae-RanAhnn, Joohong
Issue Date
Nov-2007
Publisher
WILEY
Keywords
inorganic pyrophosphatase; PYP-1; deletion mutant; larval arrest; C. elegans
Citation
FEBS LETTERS, v.581, no.28, pp.5445 - 5453
Indexed
SCIE
SCOPUS
Journal Title
FEBS LETTERS
Volume
581
Number
28
Start Page
5445
End Page
5453
URI
https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/179417
DOI
10.1016/j.febslet.2007.10.047
ISSN
0014-5793
Abstract
Inorganic pyrophosphatase ( PPase) catalyzes the hydrolysis of inorganic pyrophosphate (PPi) into phosphate ( Pi), which provides a thermodynamic driving force for important biosynthetic reactions. The nematode Caenorhabditis elegans gene C47E12.4 encodes a PPase (PYP-1) which shows 54% amino acid identity with human PPase. PYP-1 exhibits specific enzyme activity and is mainly expressed in the intestinal and nervous system. A null mutant of pyp-1 reveals a developmental arrest at early larval stages and exhibits gross defects in intestinal morphology and function. The larval arrest phenotype was successfully rescued by reintroduction of the pyp-1 gene, suggesting that PYP-1 is required for larval development and intestinal function in C. elegans.
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