Interaction of the molecular chaperone HtpG with uroporphyrinogen decarboxylase in the cyanobacterium Synechococcus elongatus PCC 7942.
Uroporphyrinogen decarboxylase (HemE) is important due to its location at the first branch-point in tetrapyrrole biosynthesis. We detected a complex formation between full-length polypeptides of HtpG and HemE by biochemical studies in vivo and in vitro. The interaction suppressed the enzyme activity, suggesting a regulatory role of HtpG in tetrapyrrole biosynthesis.
Saito
Masakazu
M
Department of Biochemistry and Molecular Biology, Saitama University, Japan.
Watanabe
Satoru
S
Yoshikawa
Hirofumi
H
Nakamoto
Hitoshi
H
D001426:Bacterial Proteins / Q000378:metabolism*; D018841:HSP90 Heat-Shock Proteins / Q000378:metabolism*; D010455:Peptides / Q000378:metabolism; D011485:Protein Binding; D046940:Synechococcus / Q000145:classification / Q000201:enzymology / Q000378:metabolism*; D045725:Tetrapyrroles / Q000378:metabolism; D014575:Uroporphyrinogen Decarboxylase / Q000378:metabolism*
D001426:Bacterial Proteins; D018841:HSP90 Heat-Shock Proteins; D010455:Peptides; D045725:Tetrapyrroles; C066720:HtpG protein, bacteria; D014575:Uroporphyrinogen Decarboxylase