Abstract:
:The fluorescence characteristics of brevin and the effects of Ca2+ on the protein conformation were fully investigated. Brevin contains 18 tryptophans and 27 tyrosines. Analysis of the fluorescence spectra and the accessibility to quenching molecules indicate that the emitting tryptophans are located in a hydrophobic environment (lambda max = 324 nm) close to the protein surface. In native brevin, tyrosyl residues do not contribute to the fluorescence emission. Partial quenching of these chromophores has to be attributed to tyrosine----tryptophan resonance energy transfer which is highly efficient. The effect of brevin on actin polymerization has been shown to be Ca2+ sensitive [Harris, D. A., & Schwartz, J. H. (1981) Proc. Natl. Acad. Sci. U.S.A. 78, 6798-6802; Thorstensson, R., Utter, G., & Norberg, R. (1982) Eur. J. Biochem. 126, 11-16; Wilkins, J. A., Schwartz, J. H. & Harris, D. A. (1983) Cell Biol. Int. Rep. 7, 1097-1104; Harris, H. E., & Weeds, A. G. (1983) Biochemistry 22, 2728-2741] and brevin binding to hydrophobic matrices to be Ca2+ dependent (Z. Soua, personal communication). Ca2+ binding to brevin decreases the tryptophan fluorescence polarization degree (without affecting the excited-state lifetime), which suggests a higher chromophore mobility. This effect may be partly related to the slight unshielding of the tryptophan residues observed in fluorescence quenching experiments. Moreover, the reactivity of brevin sulfhydryl groups toward 5,5'-dithiobis(2-nitrobenzoic acid) increases in the presence of Ca2+. On the other hand, fluorescence spectra, quantum yields, excited-state lifetimes, and thermostability remain unchanged.(ABSTRACT TRUNCATED AT 250 WORDS)
journal_name
Biochemistryjournal_title
Biochemistryauthors
Kilhoffer MC,Gérard Ddoi
10.1021/bi00341a055subject
Has Abstractpub_date
1985-09-24 00:00:00pages
5653-60issue
20eissn
0006-2960issn
1520-4995journal_volume
24pub_type
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