A pollen-specific calmodulin-binding protein, NPG1, interacts with putative pectate lyases.

Abstract:

:Previous genetic studies have revealed that a pollen-specific calmodulin-binding protein, No Pollen Germination 1 (NPG1), is required for pollen germination. However, its mode of action is unknown. Here we report direct interaction of NPG1 with pectate lyase-like proteins (PLLs). A truncated form of AtNPG1 lacking the N-terminal tetratricopeptide repeat 1 (TPR1) failed to interact with PLLs, suggesting that it is essential for NPG1 interaction with PLLs. Localization studies with AtNPG1 fused to a fluorescent reporter driven by its native promoter revealed its presence in the cytosol and cell wall of the pollen grain and the growing pollen tube of plasmolyzed pollen. Together, our data suggest that the function of NPG1 in regulating pollen germination is mediated through its interaction with PLLs, which may modify the pollen cell wall and regulate pollen tube emergence and growth.

journal_name

Sci Rep

journal_title

Scientific reports

authors

Shin SB,Golovkin M,Reddy AS

doi

10.1038/srep05263

subject

Has Abstract

pub_date

2014-06-12 00:00:00

pages

5263

issn

2045-2322

pii

srep05263

journal_volume

4

pub_type

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