Structure-function analysis of Rgs1 in Magnaporthe oryzae: role of DEP domains in subcellular targeting.

ABSTRACT:

Background

Rgs1, a prototypical Regulator of G protein Signaling, negatively modulates the cyclic AMP pathway thereby influencing various aspects of asexual development and pathogenesis in the rice-blast fungus Magnaporthe oryzae. Rgs1 possesses tandem DEP motifs (termed DEP-A and DEP-B; for Dishevelled, Egl-10, Pleckstrin) at the N-terminus, and a Gα-GTP interacting RGS catalytic core domain at the C-terminus. In this study, we focused on gaining further insights into the mechanisms of Rgs1 regulation and subcellular localization by characterizing the role(s) of the individual domains and the full-length protein during asexual development and pathogenesis in Magnaporthe.

Methodology/principal findings

Utilizing western blot analysis and specific antisera against the N- and

SUBMITTER: Ramanujam R 

PROVIDER: S-EPMC3426613 | biostudies-literature | 2012

REPOSITORIES: biostudies-literature