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Molecular cloning and disruption of a novel gene encoding UDP‐glucose:tetrahydrobiopterin α‐glucosyltransferase in the cyanobacterium Synechococcus sp. PCC 7942
Author(s) -
Choi Yong Kee,
Hwang Yoon Kyung,
Park Young Shik
Publication year - 2001
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(01)02667-9
Subject(s) - glucosyltransferase , glucosyltransferases , mutant , glycosyltransferase , gene , biochemistry , tetrahydrobiopterin , cloning (programming) , biology , synechococcus , chemistry , microbiology and biotechnology , genetics , enzyme , cyanobacteria , bacteria , cofactor , computer science , programming language
The gene encoding UDP‐glucose:tetrahydrobiopterin α‐glucosyltransferase (BGluT) was cloned from the genomic DNA of Synechococcus sp. PCC 7942. The encoded protein consisting of 359 amino acid residues was verified in vitro and in vivo to be responsible for the synthesis of tetrahydrobiopterin (BH4)‐glucoside produced in the organism. The BGluT gene is the first cloned in pteridine glycosyltransferases and also a novel one cloned so far in UDP‐glycosyltransferases. The mutant cells disrupted in the BGluT gene produced only aglycosidic BH4 at a level of 8.3% of the BH4‐glucoside in wild type cells and exhibited half of the wild type growth in normal photoautotrophic conditions. These results suggest that the glucosylation of BH4 is required for the maintenance of the high cellular concentration of the compound, thereby supporting the normal growth of Synechococcus sp. PCC 7942.