Abstract
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.
MeSH terms
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Bacterial Proteins / metabolism*
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HSP90 Heat-Shock Proteins / metabolism*
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Peptides / metabolism
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Protein Binding
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Synechococcus / classification
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Synechococcus / enzymology
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Synechococcus / metabolism*
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Tetrapyrroles / metabolism
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Uroporphyrinogen Decarboxylase / metabolism*
Substances
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Bacterial Proteins
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HSP90 Heat-Shock Proteins
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Peptides
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Tetrapyrroles
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HtpG protein, bacteria
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Uroporphyrinogen Decarboxylase