Suppression of fluorescence of tryptophan residues in proteins by replacement with 4-fluorotryptophan

The tryptophan-auxotrophic Bacillus subtilis LC33 mutant strain utilizes either tryptophan or 4-fluorotryptophan for growth. Proteins therefore could be isolated from these cells in either tryptophan-containing or 4-fluorotryptophan-containing forms. Since 4-fluorotryptophan is non-fluorescent, tryp...

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Bibliographic Details
Published in:Biochemical journal 1988-01, Vol.249 (1), p.305-308
Main Authors: Bronskill, P M, Wong, J T
Format: Article
Language:English
Subjects:
Bacillus subtilis
Bacillus subtilis - metabolism
Chromatography, High Pressure Liquid
Fluorescence
Ribosomal Proteins - metabolism
Spectrometry, Fluorescence
Tryptophan - analogs & derivatives
Tryptophan - metabolism
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Summary:The tryptophan-auxotrophic Bacillus subtilis LC33 mutant strain utilizes either tryptophan or 4-fluorotryptophan for growth. Proteins therefore could be isolated from these cells in either tryptophan-containing or 4-fluorotryptophan-containing forms. Since 4-fluorotryptophan is non-fluorescent, tryptophan fluorescence would be suppressed in the 4-fluorotryptophan-containing proteins, facilitating the investigation of other chromophores either on the proteins or interacting with the proteins. This approach, potentially applicable to any protein endogenous to or clonable into B. subtilis, was illustrated by an examination of the fluorescence of B. subtilis ribosomal proteins.
ISSN:0264-6021
1470-8728
DOI:10.1042/bj2490305