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
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).
引用
收藏
页数:5
相关论文
共 50 条
  • [21] Fidelity of seryl-tRNA synthetase to binding of natural amino acids from HierDock first principles computations
    McClendon, CL
    Vaidehi, N
    Kam, VWT
    Zhang, DQ
    Goddard, WA
    PROTEIN ENGINEERING DESIGN & SELECTION, 2006, 19 (05) : 195 - 203
  • [22] Exclusive cytosolic localization and broad tRNASer specificity of Arabidopsis thaliana seryl-tRNA synthetase
    Kekez, Mario
    Bauer, Natasa
    Saric, Ela
    Rokov-Plavec, Jasmina
    JOURNAL OF PLANT BIOLOGY, 2016, 59 (01) : 44 - 54
  • [23] Arabidopsis seryl-tRNA synthetase: the first crystal structure and novel protein interactor of plant aminoacyl-tRNA synthetase
    Kekez, Mario
    Zanki, Vladimir
    Kekez, Ivana
    Baranasic, Jurica
    Hodnik, Vesna
    Duchene, Anne-Marie
    Anderluh, Gregor
    Gruic-Sovulj, Ita
    Matkovic-Calogovic, Dubravka
    Weygand-Durasevic, Ivana
    Rokov-Plavec, Jasmina
    FEBS JOURNAL, 2019, 286 (03) : 536 - 554
  • [24] Directed Evolution of a Bacterial Leucyl tRNA in Mammalian Cells for Enhanced Noncanonical Amino Acid Mutagenesis
    Huang, Rachel L.
    Jewel, Delilah
    Kelemen, Rachel E.
    Pham, Quan
    Yared, Tarah J.
    Wang, Shu
    Singha Roy, Soumya Jyoti
    Huang, Zeyi
    Levinson, Samantha D.
    Sundaresh, Bharathi
    Miranda, Suyen Espinoza
    van Opijnen, Tim
    Chatterjee, Abhishek
    ACS SYNTHETIC BIOLOGY, 2024, 13 (07): : 2141 - 2149
  • [25] Structure-Guided Enhancement of Selectivity of Chemical Probe Inhibitors Targeting Bacterial Seryl-tRNA Synthetase
    Cain, Ricky
    Salimraj, Ramya
    Punekar, Avinash S.
    Bellini, Dom
    Fishwick, Colin W. G.
    Czaplewski, Lloyd
    Scott, David J.
    Harris, Gemma
    Dowson, Christopher G.
    Lloyd, Adrian J.
    Roper, David I.
    JOURNAL OF MEDICINAL CHEMISTRY, 2019, 62 (21) : 9703 - 9717
  • [26] Seryl-tRNA synthetase is not responsible for the evolution of CUG codon reassignment in Candida albicans
    O'Sullivan, JM
    Mihr, MJ
    Santos, MAS
    Tuite, MF
    YEAST, 2001, 18 (04) : 313 - 322
  • [27] Genomic organization, expression, and subcellular localization of mouse mitochondrial seryl-tRNA synthetase
    Gibbons, WJ
    Yan, QF
    Li, RH
    Li, XM
    Guan, MX
    BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2004, 317 (03) : 774 - 778
  • [28] Minimal tRNASer and tRNASec substrates for human seryl-tRNA synthetase:: contribution of tRNA domains to serylation and tertiary structure
    Heckl, M
    Busch, K
    Gross, HJ
    FEBS LETTERS, 1998, 427 (03): : 315 - 319
  • [29] Evolutionarily conserved cysteines in plant cytosolic seryl-tRNA synthetase are important for its resistance to oxidation
    Evic, Valentina
    Soic, Ruzica
    Mocibob, Marko
    Kekez, Mario
    Houser, Josef
    Wimmerova, Michaela
    Matkovic-Calogovic, Dubravka
    Gruic-Sovulj, Ita
    Kekez, Ivana
    Rokov-Plavec, Jasmina
    FEBS LETTERS, 2023, 597 (23) : 2975 - 2992
  • [30] Variant minihelix RNAs reveal sequence-specific recognition of the helical tRNA(Ser) acceptor stem by E-coli seryl-tRNA synthetase
    Saks, ME
    Sampson, JR
    EMBO JOURNAL, 1996, 15 (11) : 2843 - 2849