Molecular and functional properties of an archaeal phenylalanyl-tRNA synthetase from the hyperthermophile Sulfolobus solfataricus

被引：6
作者：
Lombardo, B [1 ]
Raimo, G [1 ]
Bocchini, V [1 ]
机构：
[1] Univ Naples Federico II, Dipartimento Biochim & Biotecnol Med, I-80131 Naples, Italy
来源：
BIOCHIMICA ET BIOPHYSICA ACTA-PROTEIN STRUCTURE AND MOLECULAR ENZYMOLOGY | 2002年 / 1596卷 / 02期
关键词：
archaeon; hyperthermophile; protein synthesis; phenylalanyl-tRNA synthetase; heat resistance;
D O I：
10.1016/S0167-4838(02)00223-6
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：
An archaeal phenylalanyl-tRNA synthetase (FRS) has been purified from the hyperthermophile Sulfolobus solfataricus (Ss), This enzyme is a heterotetramer made of two different subunits whose molecular mass is 56 kDa and 64 kDa, respectively. As thought, SsFRS is essential for the in vitro poly(Phe) synthesis. Interestingly, the enzyme is able to aminoacylate only endogenous tRNA but it does not seem to be a strictly ATP-dependent synthetase. SsFRS interacts with the elongation factor 1alpha isolated from the same source; this caused a significant enhancement of the SstRNA aminoacylation efficiency, thus indicating that, as well as in eukarya, in this archaeon a tRNA channelling mechanism should occur, The overall results presented in this paper show that the archaeal SsFRS behaves as the analogous enzymes isolated from eukaryal sources rather than those from eubacterial organisms. (C) 2002 Elsevier Science B.V. All rights reserved.
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页码：246 / 252
页数：7
相关论文
共 25 条
[1]   PYROPHOSPHATE-CAUSED INHIBITION OF THE AMINOACYLATION OF TRANSFER-RNA BY THE LEUCYL-TRANSFER RNA-SYNTHETASE FROM NEUROSPORA-CRASSA [J].
AIRAS, RK ;
CRAMER, F .
EUROPEAN JOURNAL OF BIOCHEMISTRY, 1986, 160 (02) :291-296
[2]   COMPARATIVE-STUDY OF SUBUNITS OF PHENYLALANYL-TRANSFER RNA-SYNTHETASE FROM ESCHERICHIA-COLI AND THERMUS-THERMOPHILUS [J].
BOBKOVA, EV ;
MASHANOVGOLIKOV, AV ;
WOLFSON, A ;
ANKILOVA, VN ;
LAVRIK, OI .
FEBS LETTERS, 1991, 290 (1-2) :95-98
[3]   Protein engineering on enzymes of the peptide elongation cycle in Sulfolobus solfataricus [J].
Bocchini, V ;
Adinolfi, BS ;
Arcari, P ;
Arcucci, A ;
Dello Russo, A ;
De Vendittis, E ;
Ianniciello, G ;
Masullo, M ;
Raimo, G .
BIOCHIMIE, 1998, 80 (11) :895-898
[4]   SEQUENCE, STRUCTURE AND EVOLUTIONARY RELATIONSHIPS BETWEEN CLASS-2 AMINOACYL-TRANSFER-RNA SYNTHETASES - AN UPDATE [J].
CUSACK, S .
BIOCHIMIE, 1993, 75 (12) :1077-1081
[5]   Phenylalanyl-tRNA synthetase from the archaeon Methanobacterium thermoautotrophicum is an (αβ)2 heterotetrameric protein [J].
Das, R ;
Vothknecht, UC .
BIOCHIMIE, 1999, 81 (11) :1037-1039
[6]   PARTITION OF TRANSFER-RNA SYNTHETASES INTO 2 CLASSES BASED ON MUTUALLY EXCLUSIVE SETS OF SEQUENCE MOTIFS [J].
ERIANI, G ;
DELARUE, M ;
POCH, O ;
GANGLOFF, J ;
MORAS, D .
NATURE, 1990, 347 (6289) :203-206
[7]   Unusual enzyme characteristics of aspartyl-tRNA synthetase from hyperthermophilic archaeon Pyrococcus sp KOD1 [J].
Fujiwara, S ;
Lee, SG ;
Haruki, M ;
Kanaya, S ;
Takagi, M ;
Imanaka, T .
FEBS LETTERS, 1996, 394 (01) :66-70
[8]   Aminoacyl-tRNA synthesis [J].
Ibba, M ;
Söll, D .
ANNUAL REVIEW OF BIOCHEMISTRY, 2000, 69 :617-650
[9]   POLYAMINES AND YELLOW LUPIN AMINOACYL TRANSFER RNA-SYNTHETASES - SPERMINE AND SPERMIDINE HELP TO MAINTAIN THE ACTIVE STRUCTURES OF AMINOACYL TRANSFER RNA-SYNTHETASES [J].
JAKUBOWSKI, H .
FEBS LETTERS, 1980, 109 (01) :63-66
[10]   CRUCIAL ROLE OF PYROPHOSPHATE IN THE AMINOACYLATION OF ESCHERICHIA-COLI TRANSFER RNA(PHE) BY YEAST PHENYLALANYL-TRANSFER RNA-SYNTHETASE [J].
KHVOROVA, AM ;
MOTORIN, YA ;
WOLFSON, AD .
FEBS LETTERS, 1992, 311 (02) :139-142
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