Functional characterization of the pleckstrin homology domain of a cellulose synthase from the Oomycete Saprolegnia monoica
2012 (English)In: Biochemical and Biophysical Research Communications - BBRC, ISSN 0006-291X, E-ISSN 1090-2104, Vol. 417, no 4, 1248-1253 p.Article in journal (Refereed) Published
Some oomycetes, for instance Saprolegnia parasitica, are severe fish pathogens that cause important economic losses worldwide. Cellulose biosynthesis is a vital process for this class of microorganisms, but the corresponding molecular mechanisms are poorly understood. Of all cellulose synthesizing enzymes known, only some oomycete cellulose synthases contain a pleckstrin homology (PH) domain. Some human PH domains bind specifically to phosphoinositides, but most PH domains bind phospholipids in a non-specific manner. In addition, some PH domains interact with various proteins. Here we have investigated the function of the PH domain of cellulose synthase 2 from the oomycete Saprolegnia monoica (SmCesA2), a species closely related to S. parasitica. The SmCesA2 PH domain is similar to the C-terminal PH domain of the human protein TAPP1. It binds in vitro to phosphoinositides, F-actin and microtubules, and co-localizes with F-actin in vivo. Our results suggest a role of the SmCesA2 PH domain in the regulation, trafficking and/or targeting of the cell wall synthesizing enzyme.
Place, publisher, year, edition, pages
Academic Press, 2012. Vol. 417, no 4, 1248-1253 p.
Pleckstrin homology domain; Cellulose synthase; Cell wall biosynthesis; Oomycetes; Phosphoinositides; F-actin
Biochemistry and Molecular Biology
IdentifiersURN: urn:nbn:se:kth:diva-34284DOI: 10.1016/j.bbrc.2011.12.118ISI: 000300196100024ScopusID: 2-s2.0-84856215112OAI: oai:DiVA.org:kth-34284DiVA: diva2:420127
Updated from manuscript to article in journal.
QC 201203062011-05-312011-05-312015-10-14Bibliographically approved