메뉴 건너뛰기




Volumn 8, Issue 6, 2005, Pages 706-712

The direct genetic encoding of pyrrolysine

Author keywords

[No Author keywords available]

Indexed keywords

LYSINE; PYRROLYSINE; UNCLASSIFIED DRUG;

EID: 27844438536     PISSN: 13695274     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.mib.2005.10.009     Document Type: Review
Times cited : (99)

References (48)
  • 1
    • 0001271789 scopus 로고
    • Phylogenetic structure of the procaryotic domain: The primary kingdoms
    • C.R. Woese, and G.E. Fox Phylogenetic structure of the procaryotic domain: the primary kingdoms Proc Natl Acad Sci USA 74 1977 5088 5090
    • (1977) Proc Natl Acad Sci USA , vol.74 , pp. 5088-5090
    • Woese, C.R.1    Fox, G.E.2
  • 3
    • 0031685510 scopus 로고    scopus 로고
    • Biochemistry of methanogenesis: A tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture
    • R.K. Thauer Biochemistry of methanogenesis: a tribute to Marjory Stephenson. 1998 Marjory Stephenson Prize Lecture Microbiology 144 1998 2377 2406
    • (1998) Microbiology , vol.144 , pp. 2377-2406
    • Thauer, R.K.1
  • 4
    • 0032883772 scopus 로고    scopus 로고
    • Novel reactions involved in energy conservation by methanogenic archaea
    • U. Deppenmeier, T. Lienard, and G. Gottschalk Novel reactions involved in energy conservation by methanogenic archaea FEBS Lett 457 1999 291 297
    • (1999) FEBS Lett , vol.457 , pp. 291-297
    • Deppenmeier, U.1    Lienard, T.2    Gottschalk, G.3
  • 5
    • 11144347500 scopus 로고    scopus 로고
    • The membrane-bound electron transport system of Methanosarcina species
    • U. Deppenmeier The membrane-bound electron transport system of Methanosarcina species J Bioenerg Biomembr 36 2004 55 64
    • (2004) J Bioenerg Biomembr , vol.36 , pp. 55-64
    • Deppenmeier, U.1
  • 6
    • 0037165964 scopus 로고    scopus 로고
    • A new UAG-encoded residue in the structure of a methanogen methyltransferase
    • B. Hao, W. Gong, T.K. Ferguson, C.M. James, J.A. Krzycki, and M.K. Chan A new UAG-encoded residue in the structure of a methanogen methyltransferase Science 296 2002 1462 1466
    • (2002) Science , vol.296 , pp. 1462-1466
    • Hao, B.1    Gong, W.2    Ferguson, T.K.3    James, C.M.4    Krzycki, J.A.5    Chan, M.K.6
  • 7
    • 0037166006 scopus 로고    scopus 로고
    • Pyrrolysine encoded by UAG in Archaea: Charging of a UAG-decoding specialized tRNA
    • G. Srinivasan, C.M. James, and J.A. Krzycki Pyrrolysine encoded by UAG in Archaea: charging of a UAG-decoding specialized tRNA Science 296 2002 1459 1462
    • (2002) Science , vol.296 , pp. 1459-1462
    • Srinivasan, G.1    James, C.M.2    Krzycki, J.A.3
  • 8
    • 0033005876 scopus 로고    scopus 로고
    • Enzymology of one-carbon metabolism in methanogenic pathways
    • J.G. Ferry Enzymology of one-carbon metabolism in methanogenic pathways FEMS Microbiol Rev 23 1999 13 38
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 13-38
    • Ferry, J.G.1
  • 9
    • 10044290566 scopus 로고    scopus 로고
    • Anaerobic growth of Methanosarcina acetivorans C2A on carbon monoxide: An unusual way of life for a methanogenic archaeon
    • M. Rother, and W.W. Metcalf Anaerobic growth of Methanosarcina acetivorans C2A on carbon monoxide: an unusual way of life for a methanogenic archaeon Proc Natl Acad Sci USA 101 2004 16929 16934
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 16929-16934
    • Rother, M.1    Metcalf, W.W.2
  • 10
    • 4644255236 scopus 로고    scopus 로고
    • Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases
    • J.A. Krzycki Function of genetically encoded pyrrolysine in corrinoid-dependent methylamine methyltransferases Curr Opin Chem Biol 8 2004 484 491 The possible roles of pyrrolysine in methylamine methyltransferase are discussed in this review.
    • (2004) Curr Opin Chem Biol , vol.8 , pp. 484-491
    • Krzycki, J.A.1
  • 11
    • 14444276994 scopus 로고    scopus 로고
    • Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri
    • D.J. Ferguson Jr., and J.A. Krzycki Reconstitution of trimethylamine-dependent coenzyme M methylation with the trimethylamine corrinoid protein and the isozymes of methyltransferase II from Methanosarcina barkeri J Bacteriol 179 1997 846 852
    • (1997) J Bacteriol , vol.179 , pp. 846-852
    • Ferguson Jr., D.J.1    Krzycki, J.A.2
  • 12
    • 0034666012 scopus 로고    scopus 로고
    • Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri
    • D.J. Ferguson Jr., N. Gorlatova, D.A. Grahame, and J.A. Krzycki Reconstitution of dimethylamine:coenzyme M methyl transfer with a discrete corrinoid protein and two methyltransferases purified from Methanosarcina barkeri J Biol Chem 275 2000 29053 29060
    • (2000) J Biol Chem , vol.275 , pp. 29053-29060
    • Ferguson Jr., D.J.1    Gorlatova, N.2    Grahame, D.A.3    Krzycki, J.A.4
  • 13
    • 0030946069 scopus 로고    scopus 로고
    • Reconstitution of monomethylamine:coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri
    • S.A. Burke, and J.A. Krzycki Reconstitution of monomethylamine:coenzyme M methyl transfer with a corrinoid protein and two methyltransferases purified from Methanosarcina barkeri J Biol Chem 272 1997 16570 16577
    • (1997) J Biol Chem , vol.272 , pp. 16570-16577
    • Burke, S.A.1    Krzycki, J.A.2
  • 14
    • 0028983268 scopus 로고
    • Involvement of the "a" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine
    • S.A. Burke, and J.A. Krzycki Involvement of the "A" isozyme of methyltransferase II and the 29-kilodalton corrinoid protein in methanogenesis from monomethylamine J Bacteriol 177 1995 4410 4416
    • (1995) J Bacteriol , vol.177 , pp. 4410-4416
    • Burke, S.A.1    Krzycki, J.A.2
  • 15
    • 0029864728 scopus 로고    scopus 로고
    • Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri
    • D.J. Ferguson Jr., J.A. Krzycki, and D.A. Grahame Specific roles of methylcobamide:coenzyme M methyltransferase isozymes in metabolism of methanol and methylamines in Methanosarcina barkeri J Biol Chem 271 1996 5189 5194
    • (1996) J Biol Chem , vol.271 , pp. 5189-5194
    • Ferguson Jr., D.J.1    Krzycki, J.A.2    Grahame, D.A.3
  • 16
    • 0034005319 scopus 로고    scopus 로고
    • The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons
    • L. Paul, D.J. Ferguson, and J.A. Krzycki The trimethylamine methyltransferase gene and multiple dimethylamine methyltransferase genes of Methanosarcina barkeri contain in-frame and read-through amber codons J Bacteriol 182 2000 2520 2529
    • (2000) J Bacteriol , vol.182 , pp. 2520-2529
    • Paul, L.1    Ferguson, D.J.2    Krzycki, J.A.3
  • 17
    • 0031799184 scopus 로고    scopus 로고
    • Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine
    • S.A. Burke, S.L. Lo, and J.A. Krzycki Clustered genes encoding the methyltransferases of methanogenesis from monomethylamine J Bacteriol 180 1998 3432 3440
    • (1998) J Bacteriol , vol.180 , pp. 3432-3440
    • Burke, S.A.1    Lo, S.L.2    Krzycki, J.A.3
  • 21
    • 20144384309 scopus 로고    scopus 로고
    • Pyrrolysine and selenocysteine use dissimilar decoding strategies
    • Y. Zhang, P.V. Baranov, J.F. Atkins, and V.N. Gladyshev Pyrrolysine and selenocysteine use dissimilar decoding strategies J Biol Chem 280 2005 20740 20751 A bioinformatic study of pyrrolysine related genes in published genome sequences. The authors collate previous information and discuss possible modes by which UAG might be decoded as pyrrolysine. Unlike selenocysteine proteins, of which many novel examples have been identified by bioinformatic approaches, new pyrrolysine genes could not be identified by common signals found following the UAG codon. The authors propose that differences between the two non-canonical coding strategies might exist.
    • (2005) J Biol Chem , vol.280 , pp. 20740-20751
    • Zhang, Y.1    Baranov, P.V.2    Atkins, J.F.3    Gladyshev, V.N.4
  • 22
    • 0035823612 scopus 로고    scopus 로고
    • The amber codon in the gene encoding the monomethylamine methyltransferase isolated from Methanosarcina barkeri is translated as a sense codon
    • C.M. James, T.K. Ferguson, J.F. Leykam, and J.A. Krzycki The amber codon in the gene encoding the monomethylamine methyltransferase isolated from Methanosarcina barkeri is translated as a sense codon J Biol Chem 276 2001 34252 34258
    • (2001) J Biol Chem , vol.276 , pp. 34252-34258
    • James, C.M.1    Ferguson, T.K.2    Leykam, J.F.3    Krzycki, J.A.4
  • 25
    • 0037165968 scopus 로고    scopus 로고
    • The 22nd amino acid
    • J.F. Atkins, and R. Gesteland The 22nd amino acid Science 296 2002 1409 1411
    • (2002) Science , vol.296 , pp. 1409-1411
    • Atkins, J.F.1    Gesteland, R.2
  • 27
    • 0345436050 scopus 로고    scopus 로고
    • Selenocysteine inserting tRNAs: An overview
    • S. Commans, and A. Bock Selenocysteine inserting tRNAs: an overview FEMS Microbiol Rev 23 1999 335 351
    • (1999) FEMS Microbiol Rev , vol.23 , pp. 335-351
    • Commans, S.1    Bock, A.2
  • 28
    • 0041317009 scopus 로고    scopus 로고
    • Mechanism and regulation of selenoprotein synthesis
    • D.M. Driscoll, and P.R. Copeland Mechanism and regulation of selenoprotein synthesis Annu Rev Nutr 23 2003 17 40
    • (2003) Annu Rev Nutr , vol.23 , pp. 17-40
    • Driscoll, D.M.1    Copeland, P.R.2
  • 30
    • 4944265620 scopus 로고    scopus 로고
    • Molecular biology: Genetic code seizes pyrrolysine
    • ••] that discusses some of the broader issues of UAG translation as pyrrolysine in light of the discovery of the pyrrolysyl-tRNA synthetase.
    • (2004) Nature , vol.431 , pp. 257-258
    • Schimmel, P.1    Beebe, K.2
  • 34
    • 0032553449 scopus 로고    scopus 로고
    • Higher-order structure and thermal instability of bovine mitochondrial tRNASerUGA investigated by proton NMR spectroscopy
    • I. Hayashi, G. Kawai, and K. Watanabe Higher-order structure and thermal instability of bovine mitochondrial tRNASerUGA investigated by proton NMR spectroscopy J Mol Biol 284 1998 57 69
    • (1998) J Mol Biol , vol.284 , pp. 57-69
    • Hayashi, I.1    Kawai, G.2    Watanabe, K.3
  • 35
    • 7444263987 scopus 로고    scopus 로고
    • An expanding genetic code
    • T.A. Cropp, and P.G. Schultz An expanding genetic code Trends Genet 20 2004 625 630
    • (2004) Trends Genet , vol.20 , pp. 625-630
    • Cropp, T.A.1    Schultz, P.G.2
  • 36
    • 19944424477 scopus 로고    scopus 로고
    • Genetic, physiological and biochemical characterization of multiple methanol methyltransferase isozymes in Methanosarcina acetivorans C2A
    • M.A. Pritchett, and W.W. Metcalf Genetic, physiological and biochemical characterization of multiple methanol methyltransferase isozymes in Methanosarcina acetivorans C2A Mol Microbiol 56 2005 1183 1194
    • (2005) Mol Microbiol , vol.56 , pp. 1183-1194
    • Pritchett, M.A.1    Metcalf, W.W.2
  • 37
    • 0035015556 scopus 로고    scopus 로고
    • Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region
    • M. Rother, A. Resch, W.L. Gardner, W.B. Whitman, and A. Bock Heterologous expression of archaeal selenoprotein genes directed by the SECIS element located in the 3′ non-translated region Mol Microbiol 40 2001 900 908
    • (2001) Mol Microbiol , vol.40 , pp. 900-908
    • Rother, M.1    Resch, A.2    Gardner, W.L.3    Whitman, W.B.4    Bock, A.5
  • 38
    • 0027282772 scopus 로고
    • Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons
    • M.J. Berry, L. Banu, J.W. Harney, and P.R. Larsen Functional characterization of the eukaryotic SECIS elements which direct selenocysteine insertion at UGA codons EMBO J 12 1993 3315 3322
    • (1993) EMBO J , vol.12 , pp. 3315-3322
    • Berry, M.J.1    Banu, L.2    Harney, J.W.3    Larsen, P.R.4
  • 40
    • 0842267214 scopus 로고    scopus 로고
    • Reprogrammed genetic decoding in cellular gene expression
    • O. Namy, J.P. Rousset, S. Napthine, and I. Brierley Reprogrammed genetic decoding in cellular gene expression Mol Cell 13 2004 157 168 The authors of this review propose that UAG decoding as pyrrolysine might involve a structural element 3′ of the UAG codon in mtmB genes. They noted that similar stem-loops could be identified in the mtmB1 and mtmB2 genes from different species. This provides a target for future mutagenesis studies aiming at elucidating the requirement context of UAG translation.
    • (2004) Mol Cell , vol.13 , pp. 157-168
    • Namy, O.1    Rousset, J.P.2    Napthine, S.3    Brierley, I.4
  • 42
    • 11144357971 scopus 로고    scopus 로고
    • Aminoacyl-tRNAs: Setting the limits of the genetic code
    • M. Ibba, and D. Söll Aminoacyl-tRNAs: setting the limits of the genetic code Genes Dev 18 2004 731 738
    • (2004) Genes Dev , vol.18 , pp. 731-738
    • Ibba, M.1    Söll, D.2
  • 45
    • 0343618479 scopus 로고    scopus 로고
    • Footprints of aminoacyl-tRNA synthetases are everywhere
    • P. Schimmel, and L. Ribas De Pouplana Footprints of aminoacyl-tRNA synthetases are everywhere Trends Biochem Sci 25 2000 207 209
    • (2000) Trends Biochem Sci , vol.25 , pp. 207-209
    • Schimmel, P.1    Ribas De Pouplana, L.2
  • 46
    • 27844607713 scopus 로고    scopus 로고
    • Characterization of a Methanosarcina acetivorans mutant unable to translate UAG as pyrrolysine
    • in press.
    • Mahapatra A, Patel A, Zhang J, Metcalf W, Krzycki J: Characterization of a Methanosarcina acetivorans mutant unable to translate UAG as pyrrolysine. Mol Microbiol 2005, in press. A 0.75 kb deletion of the pylT gene and the pyl promoter resulted in the specific loss of the ability to assimilate nitrogen or to make methane from any methylamine. The mutant possessed no detectable mtmB gene product as either full or amber-truncated MtmB. In contrast, growth on methanol or acetate was unaffected. This study reveals that pyrrolysine is not essential for growth on non-methylamine substrates, which further supports the unique relationship between methylamine metabolism and pyrrolysine.
    • (2005) Mol Microbiol
    • Mahapatra, A.1    Patel, A.2    Zhang, J.3    Metcalf, W.4    Krzycki, J.5
  • 47
    • 27844593227 scopus 로고    scopus 로고
    • A computational method to predict genetically encoded rare amino acids in proteins
    • B.N. Chaudhuri, and T.O. Yeates A computational method to predict genetically encoded rare amino acids in proteins Genome Biol 6 2005 R79 A new computational algorithm was used to find novel examples of possible pyrrolysine candidates in selected genomes. Aside from methylamine methyltransferases, the method found several other proteins, such as a cobamide biosynthetic protein, which might have a translated amber codon. These proteins might indicate novel instances of pyrrolysine utilization, but might also indicate the presence of tolerance of selected amber mutants in some genes in a microbe that is capable of UAG translation as pyrrolysine.
    • (2005) Genome Biol , vol.6 , pp. 79
    • Chaudhuri, B.N.1    Yeates, T.O.2
  • 48
    • 24744437960 scopus 로고    scopus 로고
    • Evidence for the existence in mRNAs of a hairpin element responsible for ribosome dependent pyrrolysine insertion into proteins
    • A. Theobald-Dietrich, R. Giege, and J. Rudinger-Thirion Evidence for the existence in mRNAs of a hairpin element responsible for ribosome dependent pyrrolysine insertion into proteins Biochimie 87 2005 813 817 Several computational studies have predicted the existence of the PYLIS stem-loop in MtmB. These authors demonstrate that the stem-loop can exist in vitro under temperature and pH values that would prevail in the cytoplasm. This is a much-needed first step towards empirical evaluation of this structure's role in UAG translation with mtmB transcripts.
    • (2005) Biochimie , vol.87 , pp. 813-817
    • Theobald-Dietrich, A.1    Giege, R.2    Rudinger-Thirion, J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.