TY - JOUR
T1 - Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli
AU - Gopalan, Venkat
AU - Golbik, Ralph
AU - Schreiber, Gideon
AU - Fersht, Alan R.
AU - Altman, Sidney
N1 - Funding Information:
We are grateful to members of our laboratory, especially Drs Cecilia Guerrier-Takada and Paul Eder, for helpful discussions. We thank Donna Wesolowski for technical assistance with protein purification. V.G. acknowledges the hospitality extended to him by Sir Aaron Klug, Dr Bill Scott and several members of the Structural Studies Division, MRC Laboratory of Molecular Biology, during his stay in Cambridge. Research in the laboratory of S.A. is supported by National Institutes of Health grant GM 19422. V.G. was supported by postdoctoral fellowships from the Patrick and Catherine Donaghue Foundation for Medical Research and the Anna Fuller Fund for Cancer Research. R.G. is the recipient of an Adolf Butenandt fellowship from the Max Planck Society, Germany.
PY - 1997/4/11
Y1 - 1997/4/11
N2 - Escherichia coli ribonuclease P (RNase P), a ribonucleoprotein complex which primarily functions in tRNA biosynthesis, is composed of a catalytic RNA subunit, M1 RNA, and a protein cofactor, C5 protein. The fluorescence emission spectrum of the single tryptophan residue-containing C5 protein exhibits maxima at 318 nm and 332 nm. Based on a comparison of the emission spectra of wild-type C5 protein and some of its mutant derivatives, we have determined that the 318 nm maximum could be the result of a complex formed in the excited state as a result of hydrophobic interactions between Trp109, Phe18 and Phe73. The analogous tryptophan fluorescence emission spectra of wild-type C5 protein and the barstar mutant W38F/W44F, taken together with the detailed structural information available for barstar, provide a possible explanation for the unusual emission spectrum of C5 protein.
AB - Escherichia coli ribonuclease P (RNase P), a ribonucleoprotein complex which primarily functions in tRNA biosynthesis, is composed of a catalytic RNA subunit, M1 RNA, and a protein cofactor, C5 protein. The fluorescence emission spectrum of the single tryptophan residue-containing C5 protein exhibits maxima at 318 nm and 332 nm. Based on a comparison of the emission spectra of wild-type C5 protein and some of its mutant derivatives, we have determined that the 318 nm maximum could be the result of a complex formed in the excited state as a result of hydrophobic interactions between Trp109, Phe18 and Phe73. The analogous tryptophan fluorescence emission spectra of wild-type C5 protein and the barstar mutant W38F/W44F, taken together with the detailed structural information available for barstar, provide a possible explanation for the unusual emission spectrum of C5 protein.
KW - Hydrophobic interactions
KW - RNase P protein subunit
KW - Trp fluorescence
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U2 - 10.1006/jmbi.1997.0907
DO - 10.1006/jmbi.1997.0907
M3 - Editorial
C2 - 9135109
AN - SCOPUS:0031564612
VL - 267
SP - 765
EP - 769
JO - Journal of Molecular Biology
JF - Journal of Molecular Biology
SN - 0022-2836
IS - 4
ER -