In vivo distribution of phosphothioredoxin and thioredoxin in Escherichia coli
The phosphorylation state of thioredoxin was compared in intact cells and in crude extracts. In crude extracts, the extent of phosphorylation was 0.70 to 0.80 mol of phosphate per mol of thioredoxin, with approximately equal amounts of thioredoxin phosphorylated either on cysteinyl32 (formula: see t...
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Published in | The Journal of biological chemistry Vol. 253; no. 16; pp. 5568 - 5572 |
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Main Authors | , |
Format | Journal Article |
Language | English |
Published |
United States
American Society for Biochemistry and Molecular Biology
25.08.1978
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Subjects | |
Online Access | Get full text |
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Summary: | The phosphorylation state of thioredoxin was compared in intact cells and in crude extracts. In crude extracts, the extent
of phosphorylation was 0.70 to 0.80 mol of phosphate per mol of thioredoxin, with approximately equal amounts of thioredoxin
phosphorylated either on cysteinyl32 (formula: see text) or on cysteinyl35 (formula: see text). By comparison, the extent
of thioredoxin phosphorylation in intact cells was nearly 1.0 with phosphate present almost exclusively on cysteine32. Nonphosphorylated
thioredoxin was present as the reduced thiol form (formula: see text). These findings imply that (formula: see text) is the
relevant in vivo species and that a mechanism is operative in crude extracts for transfer of phosphate from cysteine32 to
cysteine35. |
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Bibliography: | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 |
ISSN: | 0021-9258 1083-351X |
DOI: | 10.1016/S0021-9258(17)30304-6 |