Putative calmodulin-binding domains in aflatoxin biosynthesis-regulatory proteins.

Published

Journal Article

The inhibition of aflatoxin production by trifluoperazine, an anticalmodulin (CaM) agent and the relevance of Ca(2+)/CaM-dependent phosphorylation and dephosphorylation during aflatoxin biosynthesis was previously reported. To identify proteins that may be regulated by CaM, an in silico analysis for putative CaM-binding domains (CaMBDs) in the aflatoxin-related proteins of Aspergillus parasiticus was performed using the CaM target database. Interestingly, the key regulators of aflatoxin biosynthesis such as AflR and AflJ contained predicted CaMBDs at their C-termini. Furthermore, potential phosphorylation sites for CaM-kinase II were present within these CaMBDs. In addition to other aflatoxin biosynthesis enzymes--such as Vbs, DmtA and OmtA, and the VeA protein (known to regulate the expression of AflJ and AflR)--also showed the presence of putative CaMBDs. Although the present report reaffirms earlier observations on CaM-mediated regulation of aflatoxin biosynthesis, it also opens new avenues for identifying the specific targets of CaM and elucidating the exact mechanism of initiation and regulation of aflatoxin biosynthesis.

Full Text

Duke Authors

Cited Authors

  • Juvvadi, PR; Chivukula, S

Published Date

  • June 2006

Published In

Volume / Issue

  • 52 / 6

Start / End Page

  • 493 - 496

PubMed ID

  • 16732462

Pubmed Central ID

  • 16732462

International Standard Serial Number (ISSN)

  • 0343-8651

Digital Object Identifier (DOI)

  • 10.1007/s00284-005-0389-z

Language

  • eng

Conference Location

  • United States