메뉴 건너뛰기




Volumn 11, Issue 1, 2005, Pages 107-113

Structure-function analysis of the yeast NAD+-dependent tRNA 2′-phosphotransferase Tpt1

Author keywords

Mutagenics; Nicotinamide adenine dinucleotide; Phosphoryl transfer; tRNA splicing

Indexed keywords

2' PHOSPHOTRANSFERASE; ADENOSINE DIPHOSPHATE RIBOSE; ALANINE; AMINO ACID; ARGININE; HISTIDINE; NICOTINAMIDE; NICOTINAMIDE ADENINE DINUCLEOTIDE; PHOSPHOTRANSFERASE; TRANSFER RNA; UNCLASSIFIED DRUG;

EID: 11144324460     PISSN: 13558382     EISSN: None     Source Type: Journal    
DOI: 10.1261/rna.7193705     Document Type: Article
Times cited : (29)

References (26)
  • 2
    • 0025743997 scopus 로고
    • Deletion analysis of a multifunctional yeast tRNA ligase polypeptide: Identification of essential and dispensable functional domains
    • Apostol, B.L., Westaway, S.K., Abelson, J., and Greer, C.L. 1991. Deletion analysis of a multifunctional yeast tRNA ligase polypeptide: Identification of essential and dispensable functional domains. J. Biol. Chem. 266: 7445-7455.
    • (1991) J. Biol. Chem. , vol.266 , pp. 7445-7455
    • Apostol, B.L.1    Westaway, S.K.2    Abelson, J.3    Greer, C.L.4
  • 4
    • 1642297558 scopus 로고    scopus 로고
    • Structural basis for the mechanism and regulation of Sir2 enzymes
    • Avalos, J.L., Boeke, J.D., and Wolberger, C. 2004. Structural basis for the mechanism and regulation of Sir2 enzymes. Mol. Cell 13: 639-648.
    • (2004) Mol. Cell , vol.13 , pp. 639-648
    • Avalos, J.L.1    Boeke, J.D.2    Wolberger, C.3
  • 5
    • 0030031666 scopus 로고    scopus 로고
    • Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide
    • Bell, C.E. and Eisenberg, D. 1996. Crystal structure of diphtheria toxin bound to nicotinamide adenine dinucleotide. Biochemistry 35: 1137-1149.
    • (1996) Biochemistry , vol.35 , pp. 1137-1149
    • Bell, C.E.1    Eisenberg, D.2
  • 6
    • 1842333250 scopus 로고    scopus 로고
    • Mutational analysis of 39 residues of vaccinia DNA topoisomerase identifies Lys-220, Arg-223, and Asn-228 as important for covalent catalysis
    • Cheng, C., Wang, L.K., Sekiguchi, J., and Shuman, S. 1997. Mutational analysis of 39 residues of vaccinia DNA topoisomerase identifies Lys-220, Arg-223, and Asn-228 as important for covalent catalysis. J. Biol. Chem. 272: 8263-8269.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8263-8269
    • Cheng, C.1    Wang, L.K.2    Sekiguchi, J.3    Shuman, S.4
  • 8
    • 0030949354 scopus 로고    scopus 로고
    • A 2′-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae
    • Culver, G.M., McCraith, S.M., Consaul, S.A., Stanford, D.R., and Phizicky, E.M. 1997. A 2′-phosphotransferase implicated in tRNA splicing is essential in Saccharomyces cerevisiae. J. Biol. Chem. 272: 13203-13210.
    • (1997) J. Biol. Chem. , vol.272 , pp. 13203-13210
    • Culver, G.M.1    McCraith, S.M.2    Consaul, S.A.3    Stanford, D.R.4    Phizicky, E.M.5
  • 9
    • 0020618208 scopus 로고
    • Mechanism of action of a yeast RNA ligase in tRNA splicing
    • Greer, C.L., Peebles, C.L., Gegenheimer, P., and Abelson J. 1983. Mechanism of action of a yeast RNA ligase in tRNA splicing. Cell 32: 537-546.
    • (1983) Cell , vol.32 , pp. 537-546
    • Greer, C.L.1    Peebles, C.L.2    Gegenheimer, P.3    Abelson, J.4
  • 10
    • 0038228666 scopus 로고    scopus 로고
    • X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes
    • Håkansson, K., Doherty, A.J., Shuman, S., and Wigley, D.B. 1997. X-ray crystallography reveals a large conformational change during guanyl transfer by mRNA capping enzymes. Cell 89: 545-553.
    • (1997) Cell , vol.89 , pp. 545-553
    • Håkansson, K.1    Doherty, A.J.2    Shuman, S.3    Wigley, D.B.4
  • 11
    • 0033634688 scopus 로고    scopus 로고
    • Catalytic mechanism of DNA topoisomerase IB
    • Krogh, B.O. and Shuman, S. 2000. Catalytic mechanism of DNA topoisomerase IB. Mol. Cell 5: 1035-1041.
    • (2000) Mol. Cell , vol.5 , pp. 1035-1041
    • Krogh, B.O.1    Shuman, S.2
  • 12
    • 0037155171 scopus 로고    scopus 로고
    • Proton relay mechanism of general acid catalysis by DNA topoisomerase IB
    • -. 2002. Proton relay mechanism of general acid catalysis by DNA topoisomerase IB. J. Biol. Chem. 277: 5711-5714.
    • (2002) J. Biol. Chem. , vol.277 , pp. 5711-5714
  • 13
    • 0033634655 scopus 로고    scopus 로고
    • Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining
    • Odell, M., Sriskanda, V., Shuman, S., and Nikolov, D. 2000. Crystal structure of eukaryotic DNA ligase-adenylate illuminates the mechanism of nick sensing and strand joining. Mol. Cell 6: 1183-1193.
    • (2000) Mol. Cell , vol.6 , pp. 1183-1193
    • Odell, M.1    Sriskanda, V.2    Shuman, S.3    Nikolov, D.4
  • 14
    • 0020710638 scopus 로고
    • Precise excision of intervening sequences from precursor tRNAs by a membrane-associated yeast endonuclease
    • Peebles, C.L., Gegenheimer, P., and Abelson, J. 1983. Precise excision of intervening sequences from precursor tRNAs by a membrane-associated yeast endonuclease. Cell 32: 525-536.
    • (1983) Cell , vol.32 , pp. 525-536
    • Peebles, C.L.1    Gegenheimer, P.2    Abelson, J.3
  • 15
    • 0001005285 scopus 로고    scopus 로고
    • Ribonuclease A
    • Raines, R.T. 1998. Ribonuclease A. Chem. Rev. 98: 1045-1065.
    • (1998) Chem. Rev. , vol.98 , pp. 1045-1065
    • Raines, R.T.1
  • 17
    • 0242582918 scopus 로고    scopus 로고
    • Genetic and biochemical analysis of the functional domains of yeast tRNA ligase
    • Sawaya, R., Schwer, B., and Shuman, S. 2003. Genetic and biochemical analysis of the functional domains of yeast tRNA ligase. J. Biol. Chem. 278: 43298-43398.
    • (2003) J. Biol. Chem. , vol.278 , pp. 43298-43398
    • Sawaya, R.1    Schwer, B.2    Shuman, S.3
  • 18
  • 19
    • 0031453506 scopus 로고    scopus 로고
    • A conditional lethal yeast phosphotransferase mutant accumulates tRNA with a 2′-phosphate and an unmodified base at the splice junction
    • Spinelli, S.L., Consaul, S.A., and Phizicky, E.M. 1997. A conditional lethal yeast phosphotransferase mutant accumulates tRNA with a 2′-phosphate and an unmodified base at the splice junction. RNA 3: 1388-1400.
    • (1997) RNA , vol.3 , pp. 1388-1400
    • Spinelli, S.L.1    Consaul, S.A.2    Phizicky, E.M.3
  • 20
    • 0032564481 scopus 로고    scopus 로고
    • A functional homolog of a yeast tRNA splicing enzyme is conserved in higher eukaryotes and in Escherichia coli
    • Spinelli, S.L., Malik, H.S., Consaul, S.A., and Phizicky, E.M. 1998. A functional homolog of a yeast tRNA splicing enzyme is conserved in higher eukaryotes and in Escherichia coli. Proc. Natl. Acad. Sci. 95: 14136-14141.
    • (1998) Proc. Natl. Acad. Sci. , vol.95 , pp. 14136-14141
    • Spinelli, S.L.1    Malik, H.S.2    Consaul, S.A.3    Phizicky, E.M.4
  • 21
    • 0033614032 scopus 로고    scopus 로고
    • Transient ADP-ribosylation of a 2′-phosphate implicated in its removal from ligated tRNA during splicing in yeast
    • Spinelli, S.L., Kierzek, R., Turner, D.H., and Phizicky, E.M. 1999. Transient ADP-ribosylation of a 2′-phosphate implicated in its removal from ligated tRNA during splicing in yeast. J. Biol. Chem. 274: 2637-2644.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2637-2644
    • Spinelli, S.L.1    Kierzek, R.2    Turner, D.H.3    Phizicky, E.M.4
  • 22
    • 0035923435 scopus 로고    scopus 로고
    • Substrate recognition by a yeast 2′-phosphotransferase involved in tRNA splicing and its Escherichia coli homolog
    • Steiger, M.A., Kierzek, R., Turner, D.H., and Phizicky, E.M. 2001. Substrate recognition by a yeast 2′-phosphotransferase involved in tRNA splicing and its Escherichia coli homolog. Biochemistry 40: 14098-14105.
    • (2001) Biochemistry , vol.40 , pp. 14098-14105
    • Steiger, M.A.1    Kierzek, R.2    Turner, D.H.3    Phizicky, E.M.4
  • 23
    • 11144258833 scopus 로고    scopus 로고
    • Analysis of 2′-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: Evidence for a conserved two-step reaction mechanism
    • this issue
    • Steiger, M.A., Jackman, J.E., and Phizicky, E.M. 2005. Analysis of 2′-phosphotransferase (Tpt1p) from Saccharomyces cerevisiae: Evidence for a conserved two-step reaction mechanism. RNA (this issue).
    • (2005) RNA
    • Steiger, M.A.1    Jackman, J.E.2    Phizicky, E.M.3
  • 24
    • 0030730820 scopus 로고    scopus 로고
    • The yeast tRNA splicing endonuclease: A tetrameric enzyme with two active site subunits homologous to the archaeal tRNA endonucleases
    • Trotta, C.R., Miao, F., Arn, E.A., Stevens, S.W., Ho, C.K., Rauhut, R., and Abelson, J.N. 1997. The yeast tRNA splicing endonuclease: A tetrameric enzyme with two active site subunits homologous to the archaeal tRNA endonucleases. Cell 89: 849-858.
    • (1997) Cell , vol.89 , pp. 849-858
    • Trotta, C.R.1    Miao, F.2    Arn, E.A.3    Stevens, S.W.4    Ho, C.K.5    Rauhut, R.6    Abelson, J.N.7
  • 25
    • 0242626891 scopus 로고    scopus 로고
    • Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide
    • Zhao, K., Chai, X., and Marmorstein, R. 2003. Structure of the yeast Hst2 protein deacetylase in ternary complex with 2′-O-acetyl ADP ribose and histone peptide. Structure 11: 1403-1411.
    • (2003) Structure , vol.11 , pp. 1403-1411
    • Zhao, K.1    Chai, X.2    Marmorstein, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.