Functional context, biosynthesis, and genetic encoding of pyrrolysine.
Functional context, biosynthesis, and genetic encoding of pyrrolysine.
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DOI:
10.1016/j.mib.2011.04.001
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发表时间:
2011-06
影响因子:
5.4
通讯作者:
Krzycki, Joseph A.
中科院分区:
文献类型:
--
作者:
Gaston, Marsha A.;Jiang, Ruisheng;Krzycki, Joseph A.
In Methanosarcina spp., amber codons in methylamine methyltransferase genes are translated as the 22nd amino acid, pyrrolysine. The responsible pyl genes plus amber-codon containing methyltransferase genes have been identified in four archaeal and five bacterial genera, including one human pathogen. In E. coli, the recombinant pylBCD gene products biosynthesize pyrrolysine from two lysine and the pylTS gene products direct pyrrolysine incorporation into protein. In the proposed biosynthetic pathway, PylB forms methylornithine from lysine, which is joined to another lysine by PylC, and oxidized to pyrrolysine by PylD. Structures of the catalytic domain of pyrrolysyl-tRNA synthetase (archaeal PylS or bacterial PylSc) revealed binding sites for tRNAPyl and pyrrolysine. PylS and tRNAPyl are now being exploited as an orthogonal pair in recombinant systems for introduction of useful modified amino acids into proteins.
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