Open AccessIdentification of the glycosyl transferase required for synthesis of the principal glycolipid characteristic of heterocysts of Anabaena sp. strain PCC 7120
Author(s) -
Awai Koichiro,
Wolk C. Peter
Publication year - 2007
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.2006.00512.x
Subject(s) - glycolipid , heterocyst , glycosyl , nitrogenase , biology , biochemistry , transferase , cyanobacteria , curdlan , strain (injury) , mutant , anabaena , microbiology and biotechnology , enzyme , polysaccharide , nitrogen fixation , genetics , gene , bacteria , anatomy
Nitrogenase is oxygen‐labile. Cyanobacterial heterocysts can fix N 2 in an oxic milieu because their interior is micro‐oxic, for which the glycolipid layer of the heterocyst envelope is required. ORF all5341 of the Anabaena sp. genome predicts a glycosyl transferase. An insertional mutant of all5341 synthesized only a nonglycosylated form of heterocyst envelope glycolipid, and lacked a glycolipid layer. All5341 appears to be the transferase required to glycosylate the glycolipid aglycone.