Abstract
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.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 765-769 |
| Number of pages | 5 |
| Journal | Journal of Molecular Biology |
| Volume | 267 |
| Issue number | 4 |
| DOIs | |
| State | Published - Apr 11 1997 |
| Externally published | Yes |
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Keywords
- Hydrophobic interactions
- RNase P protein subunit
- Trp fluorescence
ASJC Scopus subject areas
- Virology
Cite this
Fluorescence properties of a tryptophan residue in an aromatic core of the protein subunit of ribonuclease P from Escherichia coli. / Gopalan, Venkat; Golbik, Ralph; Schreiber, Gideon; Fersht, Alan R.; Altman, Sidney.
In: Journal of Molecular Biology, Vol. 267, No. 4, 11.04.1997, p. 765-769.Research output: Contribution to journal › Article
}
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
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
UR - http://www.scopus.com/inward/record.url?scp=0031564612&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0031564612&partnerID=8YFLogxK
U2 - 10.1006/jmbi.1997.0907
DO - 10.1006/jmbi.1997.0907
M3 - Article
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 -