메뉴 건너뛰기




Volumn 210, Issue 1, 1998, Pages 85-92

A topA intein in Pyrococcus furiosus and its relatedness to the r-gyr intein of Methanococcus jannaschii

Author keywords

Intein homing; Protein splicing; Reverse gyrase; Topoisomerase

Indexed keywords

BACTERIAL ENZYME; DNA TOPOISOMERASE; ENDONUCLEASE; INTEIN; UNCLASSIFIED DRUG;

EID: 0032571440     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0378-1119(98)00044-4     Document Type: Article
Times cited : (8)

References (39)
  • 2
    • 0031039353 scopus 로고    scopus 로고
    • Characterization of the reverse gyrase from the hyperthermophilic archaeon Pyrococcus furiosus
    • Borges K.M., Bergerat A., Bogert A.M., Diruggiero J., Forterre P., Robb F.T. Characterization of the reverse gyrase from the hyperthermophilic archaeon Pyrococcus furiosus. J. Bacteriol. 179:1997;1721-1726.
    • (1997) J. Bacteriol. , vol.179 , pp. 1721-1726
    • Borges, K.M.1    Bergerat, A.2    Bogert, A.M.3    Diruggiero, J.4    Forterre, P.5    Robb, F.T.6
  • 4
    • 0030911066 scopus 로고    scopus 로고
    • Protein splicing of the Saccharomyces cerevisiae VMA intein without the endonuclease motifs
    • Chong S., Xu M.-Q. Protein splicing of the Saccharomyces cerevisiae VMA intein without the endonuclease motifs. J. Biol. Chem. 272:1997;15587-15590.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15587-15590
    • Chong, S.1    Xu, M.-Q.2
  • 6
    • 0030789206 scopus 로고    scopus 로고
    • Statistical modeling, phylogenetic analysis and structure prediction of a protein splicing domain common to inteins and hedgehog proteins
    • Dalgaard J.Z., Moser M.J., Hughey R., Mian I.S. Statistical modeling, phylogenetic analysis and structure prediction of a protein splicing domain common to inteins and hedgehog proteins. J. Comput. Biol. 4:1997;193-214.
    • (1997) J. Comput. Biol. , vol.4 , pp. 193-214
    • Dalgaard, J.Z.1    Moser, M.J.2    Hughey, R.3    Mian, I.S.4
  • 7
    • 0027972347 scopus 로고
    • Evidence of selection for protein introns in the recAs of pathogenic mycobacteria
    • Davis E.O., Thangaraj H.S., Brooks P.C., Colston M.J. Evidence of selection for protein introns in the recAs of pathogenic mycobacteria. EMBO J. 13:1994;699-703.
    • (1994) EMBO J. , vol.13 , pp. 699-703
    • Davis, E.O.1    Thangaraj, H.S.2    Brooks, P.C.3    Colston, M.J.4
  • 8
    • 0030803760 scopus 로고    scopus 로고
    • Genetic definition of a protein-splicing domain: Functional mini-inteins support structure predictions and a model for intein evolution
    • Derbyshire V., Wood D.W., Wu W., Dansereau J.T., Dalgaard J.Z., Belfort M. Genetic definition of a protein-splicing domain: functional mini-inteins support structure predictions and a model for intein evolution. Proc. Natl. Acad. Sci. USA. 94:1997;11466-11471.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 11466-11471
    • Derbyshire, V.1    Wood, D.W.2    Wu, W.3    Dansereau, J.T.4    Dalgaard, J.Z.5    Belfort, M.6
  • 9
    • 0027230552 scopus 로고
    • The comings and goings of homing endonucleases and mobile introns
    • Doolittle R.F. The comings and goings of homing endonucleases and mobile introns. Proc. Natl. Acad. Sci. USA. 90:1993;5379-5381.
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 5379-5381
    • Doolittle, R.F.1
  • 10
    • 0028966185 scopus 로고
    • Overexpression of RNase H partially complements the growth defect of an Escherichia coli topA mutant: R-loop fromation is a major problem in the absence of DNA topoisomerase I
    • Drolet M., Phoenix P., Menzel R., Masse E., Liu L.F., Crouch R.J. Overexpression of RNase H partially complements the growth defect of an Escherichia coli topA mutant: R-loop fromation is a major problem in the absence of DNA topoisomerase I. Proc. Natl. Acad. Sci. USA. 92:1995;3526-3530.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 3526-3530
    • Drolet, M.1    Phoenix, P.2    Menzel, R.3    Masse, E.4    Liu, L.F.5    Crouch, R.J.6
  • 11
    • 0030611387 scopus 로고    scopus 로고
    • Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity
    • Duan X., Gimble F.S., Quiocho F.A. Crystal structure of PI-SceI, a homing endonuclease with protein splicing activity. Cell. 89:1997;555-564.
    • (1997) Cell , vol.89 , pp. 555-564
    • Duan, X.1    Gimble, F.S.2    Quiocho, F.A.3
  • 12
    • 0029899126 scopus 로고    scopus 로고
    • A hot topic: The origin of hyperthermophiles
    • Forterre P. A hot topic: the origin of hyperthermophiles. Cell. 85:1996;789-792.
    • (1996) Cell , vol.85 , pp. 789-792
    • Forterre, P.1
  • 13
    • 0029939089 scopus 로고    scopus 로고
    • Homing events in the gyrA gene of some mycobacteria
    • Fsihi H., Vincent V., Cole S.T. Homing events in the gyrA gene of some mycobacteria. Proc. Natl. Acad. Sci. USA. 93:1996;3410-3415.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 3410-3415
    • Fsihi, H.1    Vincent, V.2    Cole, S.T.3
  • 14
    • 0026772764 scopus 로고
    • Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae
    • Gimble F.S., Thorner J. Homing of a DNA endonuclease gene by meiotic gene conversion in Saccharomyces cerevisiae. Nature. 357:1992;301-306.
    • (1992) Nature , vol.357 , pp. 301-306
    • Gimble, F.S.1    Thorner, J.2
  • 15
    • 0028947630 scopus 로고
    • Substitutions in conserved dodecapeptide motifs that uncouple the DNA binding and DNA cleavage activities of PI-SceI
    • Gimble F.S., Stephens B.W. Substitutions in conserved dodecapeptide motifs that uncouple the DNA binding and DNA cleavage activities of PI-SceI. J. Biol. Chem. 270:1995;5849-5856.
    • (1995) J. Biol. Chem. , vol.270 , pp. 5849-5856
    • Gimble, F.S.1    Stephens, B.W.2
  • 16
    • 0027405022 scopus 로고
    • Peptide splicing in the vacuolar ATPase subunit A from Candida tropicalis
    • Gu H.H., Xu J., Gallagher M., Dean G.E. Peptide splicing in the vacuolar ATPase subunit A from Candida tropicalis. J. Biol. Chem. 268:1993;7372-7381.
    • (1993) J. Biol. Chem. , vol.268 , pp. 7372-7381
    • Gu, H.H.1    Xu, J.2    Gallagher, M.3    Dean, G.E.4
  • 17
    • 0342813091 scopus 로고    scopus 로고
    • Crystal structure of a hedgehog autoprocessing domain: Homology between hedgehog and self-splicing proteins
    • Hall T.M.T., Porter J.A., Young K.E., Koonin E.V., Beachy P.A., Leahy D.J. Crystal structure of a hedgehog autoprocessing domain: homology between hedgehog and self-splicing proteins. Cell. 91:1997;85-97.
    • (1997) Cell , vol.91 , pp. 85-97
    • Hall, T.M.T.1    Porter, J.A.2    Young, K.E.3    Koonin, E.V.4    Beachy, P.A.5    Leahy, D.J.6
  • 18
    • 0025240361 scopus 로고
    • Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae
    • Hirata R., Ohsumi Y., Nakano A., Kawasaki H., Suzuki K., Anraku Y. Molecular structure of a gene, VMA1, encoding the catalytic subunit of H(+)-translocating adenosine triphosphatase from vacuolar membranes of Saccharomyces cerevisiae. J. Biol. Chem. 265:1990;6726-6733.
    • (1990) J. Biol. Chem. , vol.265 , pp. 6726-6733
    • Hirata, R.1    Ohsumi, Y.2    Nakano, A.3    Kawasaki, H.4    Suzuki, K.5    Anraku, Y.6
  • 19
    • 0025226104 scopus 로고
    • Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase
    • Kane P.M., Yamashiro C.T., Wolczyk D.F., Neff N., Goebl M., Stevens T.H. Protein splicing converts the yeast TFP1 gene product to the 69-kD subunit of the vacuolar H(+)-adenosine triphosphatase. Science. 250:1990;651-657.
    • (1990) Science , vol.250 , pp. 651-657
    • Kane, P.M.1    Yamashiro, C.T.2    Wolczyk, D.F.3    Neff, N.4    Goebl, M.5    Stevens, T.H.6
  • 20
    • 0030952831 scopus 로고    scopus 로고
    • Identification of three core regions essential for protein splicing of the yeast Vma1 protozyme
    • Kawasaki M., Nogami S., Satow Y., Ohya Y., Anraku Y. Identification of three core regions essential for protein splicing of the yeast Vma1 protozyme. J. Biol. Chem. 272:1997;15668-15674.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15668-15674
    • Kawasaki, M.1    Nogami, S.2    Satow, Y.3    Ohya, Y.4    Anraku, Y.5
  • 21
    • 0028944672 scopus 로고
    • A protein splice-junction motif in hedgehog family proteins
    • Koonin E.V. A protein splice-junction motif in hedgehog family proteins. Trends Biochem. Sci. 20:1995;141-142.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. 141-142
    • Koonin, E.V.1
  • 23
    • 0028115776 scopus 로고
    • Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I
    • Lima C.D., Wang J.C., Mondragon A. Three-dimensional structure of the 67K N-terminal fragment of E. coli DNA topoisomerase I. Nature. 367:1994;138-146.
    • (1994) Nature , vol.367 , pp. 138-146
    • Lima, C.D.1    Wang, J.C.2    Mondragon, A.3
  • 24
    • 0031587023 scopus 로고    scopus 로고
    • Identification and characterization of a cyanobacterial dnaX intein
    • Liu X.-Q., Hu Z. Identification and characterization of a cyanobacterial dnaX intein. FEBS Lett. 408:1997;311-314.
    • (1997) FEBS Lett. , vol.408 , pp. 311-314
    • Liu, X.-Q.1    Hu, Z.2
  • 25
    • 0030753081 scopus 로고    scopus 로고
    • A dnaB intein in Rhodothermus marinus: Indication of recent intein homing across remotely related organisms
    • Liu X.-Q., Hu Z. A dnaB intein in Rhodothermus marinus: indication of recent intein homing across remotely related organisms. Proc. Natl. Acad. Sci. USA. 94:1997;7851-7856.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 7851-7856
    • Liu, X.-Q.1    Hu, Z.2
  • 27
    • 0030763705 scopus 로고    scopus 로고
    • Compilation and analysis of intein sequences
    • Perler F.B., Olsen G.J., Adam E. Compilation and analysis of intein sequences. Nucleic Acids Res. 25:1997;1087-1093.
    • (1997) Nucleic Acids Res. , vol.25 , pp. 1087-1093
    • Perler, F.B.1    Olsen, G.J.2    Adam, E.3
  • 28
    • 0031028203 scopus 로고    scopus 로고
    • Roles of DNA topoisomerases in the regulation of R-loop formation in vitro
    • Phoenix P., Raymond M.-A., Masse E., Drolet M. Roles of DNA topoisomerases in the regulation of R-loop formation in vitro. J. Biol. Chem. 272:1997;1473-1479.
    • (1997) J. Biol. Chem. , vol.272 , pp. 1473-1479
    • Phoenix, P.1    Raymond, M.-A.2    Masse, E.3    Drolet, M.4
  • 29
    • 0028607524 scopus 로고
    • Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins
    • Pietrokovski S. Conserved sequence features of inteins (protein introns) and their use in identifying new inteins and related proteins. Protein Sci. 3:1994;2340-2350.
    • (1994) Protein Sci. , vol.3 , pp. 2340-2350
    • Pietrokovski, S.1
  • 30
    • 0030210936 scopus 로고    scopus 로고
    • A new intein in cyanobacteria and its significance for the spread of inteins
    • Pietrokovski S. A new intein in cyanobacteria and its significance for the spread of inteins. Trends Genet. 12:1996;287-288.
    • (1996) Trends Genet. , vol.12 , pp. 287-288
    • Pietrokovski, S.1
  • 31
    • 0031025616 scopus 로고    scopus 로고
    • Ribonucleotide reductase in the archaeon Pyrococcus furiosus: A critical enzyme in the evolution of DNA genomes?
    • Riera J., Robb F.T., Weiss R., Fontecave M. Ribonucleotide reductase in the archaeon Pyrococcus furiosus: a critical enzyme in the evolution of DNA genomes? Proc. Natl. Acad. Sci. USA. 94:1997;475-478.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 475-478
    • Riera, J.1    Robb, F.T.2    Weiss, R.3    Fontecave, M.4
  • 32
    • 0029124041 scopus 로고
    • Protein splicing: Characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence
    • Shao Y., Xu M.Q., Paulus H. Protein splicing: characterization of the aminosuccinimide residue at the carboxyl terminus of the excised intervening sequence. Biochemistry. 34:1995;10844-10850.
    • (1995) Biochemistry , vol.34 , pp. 10844-10850
    • Shao, Y.1    Xu, M.Q.2    Paulus, H.3
  • 33
    • 0030012109 scopus 로고    scopus 로고
    • Protein splicing: Evidence for an N-O acyl rearrangement as the initial step in the splicing process
    • Shao Y., Xu M.Q., Paulus H. Protein splicing: evidence for an N-O acyl rearrangement as the initial step in the splicing process. Biochemistry. 35:1996;3810-3815.
    • (1996) Biochemistry , vol.35 , pp. 3810-3815
    • Shao, Y.1    Xu, M.Q.2    Paulus, H.3
  • 34
    • 0026686361 scopus 로고
    • Protein introns: A new home for endonucleases
    • Shub D.A., Goodrich-Blair H. Protein introns: a new home for endonucleases. Cell. 71:1992;183-186.
    • (1992) Cell , vol.71 , pp. 183-186
    • Shub, D.A.1    Goodrich-Blair, H.2
  • 36
    • 0027968068 scopus 로고
    • CLUSTAL W: Improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, positions-specific gap penalties and weight matrix choice. Nucleic Acids Res. 22:1994;4673-4680.
    • (1994) Nucleic Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 37
    • 0027483414 scopus 로고
    • The curious case of protein splicing: Mechanistic insights suggested by protein semisynthesis
    • Wallace C.J. The curious case of protein splicing: mechanistic insights suggested by protein semisynthesis. Prot. Sci. 2:1993;697-705.
    • (1993) Prot. Sci. , vol.2 , pp. 697-705
    • Wallace, C.J.1
  • 38
    • 0030014783 scopus 로고    scopus 로고
    • DNA topoisomerases
    • Wang J.C. DNA topoisomerases. Annu. Rev. Biochem. 65:1996;635-692.
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 635-692
    • Wang, J.C.1
  • 39
    • 0027984269 scopus 로고
    • Protein splicing: An analysis of the branched intermediate and its resolution by succinimide formation
    • Xu M.Q., Comb D.G., Paulus H., Noren C.J., Shao Y., Perler F.B. Protein splicing: an analysis of the branched intermediate and its resolution by succinimide formation. EMBO J. 13:1994;5517-5522.
    • (1994) EMBO J. , vol.13 , pp. 5517-5522
    • Xu, M.Q.1    Comb, D.G.2    Paulus, H.3    Noren, C.J.4    Shao, Y.5    Perler, F.B.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.