An orthogonal seryl-tRNA synthetase/tRNA pair for noncanonical amino acid mutagenesis in Escherichia coli!

被引：13
作者：
Zambaldo, Claudio [1 ,2 ]
Koh, Minseob [1 ,2 ]
Nasertorabi, Fariborz [3 ,4 ]
Han, Gye Won [3 ,4 ]
Chatterjee, Abhishek [5 ]
Stevens, Raymond C. [3 ,4 ]
Schultz, Peter G. [1 ,2 ]
机构：
[1] Scripps Res Inst, Dept Chem, 10550 N Torrey Pines Rd, La Jolla, CA 92037 USA
[2] Scripps Res Inst, Skaggs Inst Chem Biol, 10550 N Torrey Pines Rd, La Jolla, CA 92037 USA
[3] Univ Southern Calif, Michelson Ctr Convergent Biosci, Bridge Inst, Dept Biol Sci, Los Angeles, CA 90089 USA
[4] Univ Southern Calif, Michelson Ctr Convergent Biosci, Bridge Inst, Dept Chem, Los Angeles, CA 90089 USA
[5] Boston Coll, Dept Chem, 2609 Beacon St,246B Merkert Chem Ctr, Chestnut Hill, MA 02467 USA
来源：
BIOORGANIC & MEDICINAL CHEMISTRY | 2020年 / 28卷 / 20期
关键词：
Seryl-tRNA synthetase; E. coli orthogonality; Genetic code expansion; X-ray crystallography; Non-canonical amino acids; GENETIC-CODE; CRYSTAL-STRUCTURE; THERMUS-THERMOPHILUS; EVOLUTION; AMBER; DISCRIMINATION; PHOSPHOSERINE; MULTIPLE; REVEALS;
D O I：
10.1016/j.bmc.2020.115662
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：
We report the development of the orthogonal amber-suppressor pair Archaeoglobus fulgidus seryl-tRNA (Af-tRNA(Ser))/Methanosarcina mazei seryl-tRNA synthetase (MmSerRS) in Escherichia coli. Furthermore, the crystal structure of MmSerRS was solved at 1.45 angstrom resolution, which should enable structure-guided engineering of its active site to genetically encode small, polar noncanonical amino acids (ncAAs).
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页数：5
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共 38 条
[1]   Adaptation of an orthogonal archaeal leucyl-tRNA and synthetase pair for four-base, amber, and opal suppression [J].
Anderson, JC ;
Schultz, PG .
BIOCHEMISTRY, 2003, 42 (32) :9598-9608
[2]   CRYSTAL-STRUCTURES AT 2.5 ANGSTROM RESOLUTION OF SERYL-TRANSFER-RNA SYNTHETASE COMPLEXED 2 ANALOGS OF SERYL ADENYLATE [J].
BELRHALI, H ;
YAREMCHUK, A ;
TUKALO, M ;
LARSEN, K ;
BERTHETCOLOMINAS, C ;
LEBERMAN, R ;
BEIJER, B ;
SPROAT, B ;
ALSNIELSEN, J ;
GRUBEL, G ;
LEGRAND, JF ;
LEHMANN, M ;
CUSACK, S .
SCIENCE, 1994, 263 (5152) :1432-1436
[3]   Structure of the unusual seryl-tRNA synthetase reveals a distinct zinc-dependent mode of substrate recognition [J].
Bilokapic, Silvija ;
Maier, Timm ;
Ahel, Dragana ;
Gruic-Sovulj, Ita ;
Soell, Dieter ;
Weygand-Durasevic, Ivana ;
Ban, Nenad .
EMBO JOURNAL, 2006, 25 (11) :2498-2509
[4]   THE 2.9 ANGSTROM CRYSTAL-STRUCTURE OF THERMUS-THERMOPHILUS SERYL-TRANSFER-RNA SYNTHETASE COMPLEXED WITH TRNA(SER) [J].
BIOU, V ;
YAREMCHUK, A ;
TUKALO, M ;
CUSACK, S .
SCIENCE, 1994, 263 (5152) :1404-1410
[5]   A Tryptophanyl-tRNA Synthetase/tRNA Pair for Unnatural Amino Acid Mutagenesis in E.coli [J].
Chatterjee, Abhishek ;
Xiao, Han ;
Yang, Peng-Yu ;
Soundararajan, Gautam ;
Schultz, Peter G. .
ANGEWANDTE CHEMIE-INTERNATIONAL EDITION, 2013, 52 (19) :5106-5109
[6]   A Versatile Platform for Single- and Multiple-Unnatural Amino Acid Mutagenesis in Escherichia coli [J].
Chatterjee, Abhishek ;
Sun, Sophie B. ;
Furman, Jennifer L. ;
Xiao, Han ;
Schultz, Peter G. .
BIOCHEMISTRY, 2013, 52 (10) :1828-1837
[7]   Evolution of multiple, mutually orthogonal prolyl-tRNA synthetase/tRNA pairs for unnatural amino acid mutagenesis in Escherichia coli [J].
Chatterjee, Abhishek ;
Xiao, Han ;
Schultz, Peter G. .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 2012, 109 (37) :14841-14846
[8]   SEQUENCE, STRUCTURAL AND EVOLUTIONARY RELATIONSHIPS BETWEEN CLASS-2 AMINOACYL-TRANSFER RNA-SYNTHETASES [J].
CUSACK, S ;
HARTLEIN, M ;
LEBERMAN, R .
NUCLEIC ACIDS RESEARCH, 1991, 19 (13) :3489-3498
[9]   A 2ND CLASS OF SYNTHETASE STRUCTURE REVEALED BY X-RAY-ANALYSIS OF ESCHERICHIA-COLI SERYL-TRANSFER RNA-SYNTHETASE AT 2.5-A [J].
CUSACK, S ;
BERTHETCOLOMINAS, C ;
HARTLEIN, M ;
NASSAR, N ;
LEBERMAN, R .
NATURE, 1990, 347 (6290) :249-255
[10]   Transfer RNA-mediated editing in threonyl-tRNA synthetase: The class II solution to the double discrimination problem [J].
Dock-Bregeon, AC ;
Sankaranarayanan, R ;
Romby, P ;
Caillet, J ;
Springer, M ;
Rees, B ;
Francklyn, CS ;
Ehresmann, C ;
Moras, D .
CELL, 2000, 103 (06) :877-884
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