Molecular heterogeneity of phospholipase D (PLD): cloning of PLDγ and regulation of plant PLDγ,-β, and-α by polyphosphoinositides and calcium
Phospholipase D (PLD) has emerged as an important enzyme involved in signal
transduction, vesicle trafficking, and membrane metabolism. This report describes the
cloning and expression of a new Arabidopsis PLD cDNA, designated PLDγ, and the
regulation of PLDγ,-β, and-α by phosphatidylinositol 4, 5-bisphosphate (PIP 2) and Ca 2+.
The PLDγ cDNA is 3.3 kilobases in length and codes for an 855-amino acid protein of
95,462 Da with a pI of 6.9. PLDγ shares a 66% amino acid sequence identity with PLDβ, but …
transduction, vesicle trafficking, and membrane metabolism. This report describes the
cloning and expression of a new Arabidopsis PLD cDNA, designated PLDγ, and the
regulation of PLDγ,-β, and-α by phosphatidylinositol 4, 5-bisphosphate (PIP 2) and Ca 2+.
The PLDγ cDNA is 3.3 kilobases in length and codes for an 855-amino acid protein of
95,462 Da with a pI of 6.9. PLDγ shares a 66% amino acid sequence identity with PLDβ, but …
Molecular heterogeneity of phospholipase D (PLD): cloning of PLDγ and regulation of plant PLDγ,-β, and-α by polyphosphoinositides.
QWS Qin WenSheng, K Pappan, WXM Wang XueMin - 1997 - cabidigitallibrary.org
Abstract Phospholipase D (PLD; EC 3.1. 4.4) is an important enzyme involved in signal
transduction, vesicle trafficking and membrane metabolism. A new Arabidopsis thaliana PLD
cDNA (PLDγ) was cloned and characterized. PLDγ is 3.3 kilobases in length and encodes
an 855-amino acid protein (95 462 Da) which shares 66% and 41% amino acid sequence
identity with A. thaliana PLDβ and PLDα, respectively. A potential N-terminal myristoylation
site was identified in PLDγ, but not in PLDα and-β. Catalytically active PLDγ was expressed …
transduction, vesicle trafficking and membrane metabolism. A new Arabidopsis thaliana PLD
cDNA (PLDγ) was cloned and characterized. PLDγ is 3.3 kilobases in length and encodes
an 855-amino acid protein (95 462 Da) which shares 66% and 41% amino acid sequence
identity with A. thaliana PLDβ and PLDα, respectively. A potential N-terminal myristoylation
site was identified in PLDγ, but not in PLDα and-β. Catalytically active PLDγ was expressed …
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