Peptides derived from Kex2-processed repeat proteins are widely distributed and highly diverse in the Fungi kingdom.

ABSTRACT:

Background

Recently, a gene cluster responsible for biosynthesis of ustiloxin in Aspergillus flavus was identified as the first case of a ribosomally synthesized and post-translationally modified peptide (RiPP) synthetic pathway in Ascomycota. RiPPs are biosynthesized from precursor peptides, which are processed to produce the RiPP backbone (core peptides) for further modifications such as methylation and cyclization. Ustiloxin precursor peptide has two distinctive features: a signal peptide for translocation into the endoplasmic reticulum and highly repeated core sequences cleaved by Kex2 protease in the Golgi apparatus. On the basis of these characteristics, the ustiloxin-type RiPP precursor peptides or Kex2-processed repeat proteins (KEPs) in strains belonging to the Fung

SUBMITTER: Umemura M 

PROVIDER: S-EPMC7329392 | biostudies-literature | 2020

REPOSITORIES: biostudies-literature