H-1-NMR AND PHOTO-CIDNP SPECTROSCOPIES SHOW A POSSIBLE ROLE FOR TRP(23) AND PHE(31) IN NUCLEIC-ACID BINDING BY P2 RIBONUCLEASE FROM THE ARCHAEON SULFOLOBUS-SOLFATARICUS

被引:7
作者
CONSONNI, R
LIMIROLI, R
MOLINARI, H
FUSI, P
GRISA, M
VANONI, M
TORTORA, P
机构
[1] UNIV VERONA,IST POLICATTEDRA,I-37134 VERONA,ITALY
[2] UNIV MILAN,DIPARTIMENTO FISIOL & BIOCHIM GEN,I-20133 MILAN,ITALY
[3] IST SPERIMENTALE ELAIOTECN,PESCARA,ITALY
关键词
ARCHAEBACTERIA; RNA RECOGNITION MOTIF; P2; NMR; PHOTO-CIDNP; SULFOLOBUS SOLFATARICUS;
D O I
10.1016/0014-5793(95)00940-B
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
Investigations were performed on recombinant ribonuclease P2 from Sulfolobus solfataricus, previously cloned and expressed in Escherichia coli [Fusi, P., Grisa, M., Mombelli, E., Consonni, R., Tortora, P. and Vanoni, M. (1995) Gene 154, 99-103], MMR and photo-CIDNP spectroscopies showed that the enzyme possesses an aromatic cluster constisting of Phe(5), Tyr(7), Phe(31) and Tyr(33) while Trp(23) is fully exposed to solvent, Phe(31), Tyr(33) and Trp(23) located within a triple stranded antiparallel beta-sheet, each one being part of an amino acid stretch matching consensus sequences for RNA binding, Phe(31) and Trp(23) are exposed to and specifically interact with a flavin dye used as a model ligand, with a topology reminiscent of that found in several eubacterial and eukariotic RNA-binding proteins.
引用
收藏
页码:135 / 139
页数:5
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