Open AccessHighly Diverse Cyanobactins in Strains of the Genus Anabaena
Author(s) -
Niina Leikoski,
David P. Fewer,
Jouni Jokela,
Matti Wahlsten,
Leo Rouhiainen,
Kaarina Sivonen
Publication year - 2010
Publication title -
applied and environmental microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.552
H-Index - 324
eISSN - 1070-6291
pISSN - 0099-2240
DOI - 10.1128/aem.01061-09
Subject(s) - biology , amino acid , genome , biochemistry , escherichia coli , heterologous expression , cyanobacteria , anabaena , heterologous , cyclic peptide , peptide sequence , gene , cleavage (geology) , bacteria , genetics , peptide , recombinant dna , paleontology , fracture (geology)
Cyanobactins are small, cyclic peptides recently found in cyanobacteria. They are formed through proteolytic cleavage and posttranslational modification of short precursor proteins and exhibit antitumor, cytotoxic, or multi-drug-reversing activities. Using genome project data, bioinformatics, stable isotope labeling, and mass spectrometry, we discovered novel cyclic peptides, anacyclamides, in 27Anabaena strains. The lengths of the anacylamides varied greatly, from 7 to 20 amino acids. Pronounced sequence variation was also detected, and only one amino acid, proline, was present in all anacyclamides. The anacyclamides identified included unmodified proteinogenic or prenylated amino acids. We identified an 11-kb gene cluster in the genome ofAnabaena sp. 90, and heterologous expression inEscherichia coli confirmed that this cluster was responsible for anacyclamide production. The discovery of anacyclamides greatly increases the structural diversity of cyanobactins.