메뉴 건너뛰기




Volumn 279, Issue 3, 1998, Pages 513-527

Recognition of core-type DNA sites by λ integrase

Author keywords

DNA binding protein; Photocrosslinking; Protein domain structure; Protein modification; Site specific recombination

Indexed keywords

ALANINE; BACTERIAL ENZYME; DNA BINDING PROTEIN; INTEGRASE; RECOMBINASE;

EID: 0032511135     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1998.1786     Document Type: Article
Times cited : (47)

References (57)
  • 1
    • 0026586392 scopus 로고
    • Evidence for a second conserved arginine residue in the integrase family of recombination proteins
    • Abremski K.E., Hoess R.H. Evidence for a second conserved arginine residue in the integrase family of recombination proteins. Protein Eng. 5:1992;87-91
    • (1992) Protein Eng. , vol.5 , pp. 87-91
    • Abremski, K.E.1    Hoess, R.H.2
  • 4
    • 0023125846 scopus 로고
    • Identification and amino acid sequence of the deoxynucleoside triphosphate binding site in Escherichia coli DNA polymerase I
    • Basu A., Modak M.J. Identification and amino acid sequence of the deoxynucleoside triphosphate binding site in Escherichia coli DNA polymerase I. Biochemistry. 26:1987;1704-1709
    • (1987) Biochemistry , vol.26 , pp. 1704-1709
    • Basu, A.1    Modak, M.J.2
  • 5
    • 0024349250 scopus 로고
    • Active-site modification of mammalian DNA polymerase B with pyridoxal 5′-phosphate: Mechanism of inhibition and identification of lysine 71 in the deoxynucleoside binding pocket
    • Basu A., Kedar P., Wilson S.H., Modak M.J. Active-site modification of mammalian DNA polymerase B with pyridoxal 5′-phosphate mechanism of inhibition and identification of lysine 71 in the deoxynucleoside binding pocket. Biochemistry. 28:1989;6305-6309
    • (1989) Biochemistry , vol.28 , pp. 6305-6309
    • Basu, A.1    Kedar, P.2    Wilson, S.H.3    Modak, M.J.4
  • 6
    • 0024324362 scopus 로고
    • Substrate binding in human immunodeficiency virus reverse transcriptase
    • Basu A., Tirumalai R.S., Modak M.J. Substrate binding in human immunodeficiency virus reverse transcriptase. J. Biol. Chem. 264:1989;8746-8752
    • (1989) J. Biol. Chem. , vol.264 , pp. 8746-8752
    • Basu, A.1    Tirumalai, R.S.2    Modak, M.J.3
  • 7
    • 0026527228 scopus 로고
    • Identification of the primer binding domain in human immunodeficiency virus reverse transcriptase
    • Basu A., Ahluwalia K.K., Basu S., Modak M.J. Identification of the primer binding domain in human immunodeficiency virus reverse transcriptase. Biochemistry. 31:1992;616-623
    • (1992) Biochemistry , vol.31 , pp. 616-623
    • Basu, A.1    Ahluwalia, K.K.2    Basu, S.3    Modak, M.J.4
  • 8
    • 0023782860 scopus 로고
    • Pyridoxal 5′-phosphate mediated inactivation of Escherichia coli DNA polymerase I: Identification of lysine-635 as an essential residue for the processive mode of DNA synthesis
    • Basu S., Basu A., Modak M.J. Pyridoxal 5′-phosphate mediated inactivation of Escherichia coli DNA polymerase I identification of lysine-635 as an essential residue for the processive mode of DNA synthesis. Biochemistry. 27:1988;6710-6716
    • (1988) Biochemistry , vol.27 , pp. 6710-6716
    • Basu, S.1    Basu, A.2    Modak, M.J.3
  • 10
    • 0029911816 scopus 로고    scopus 로고
    • Cis and trans in site-specific recombination
    • Blakely G.W., Sherratt D.J. Cis and trans in site-specific recombination. Mol. Microbiol. 20:1996;234-237
    • (1996) Mol. Microbiol. , vol.20 , pp. 234-237
    • Blakely, G.W.1    Sherratt, D.J.2
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:1976;248-254
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 13
    • 0026651559 scopus 로고
    • DNA cleavage in trans by the active site tyrosine during Flp recombination: Switching protein partners before exchanging strands
    • Chen J.-W., Lee J., Jayaram M. DNA cleavage in trans by the active site tyrosine during Flp recombination Switching protein partners before exchanging strands. Cell. 69:1992;647-658
    • (1992) Cell , vol.69 , pp. 647-658
    • Chen, J.-W.1    Lee, J.2    Jayaram, M.3
  • 14
    • 0029147088 scopus 로고
    • Identifying determinants of recombination specificity: Construction and characterization of mutant bacteriophage integrases
    • Dorgai L., Yagil E., Weisberg R.A. Identifying determinants of recombination specificity Construction and characterization of mutant bacteriophage integrases. J. Mol. Biol. 252:1995;178-188
    • (1995) J. Mol. Biol. , vol.252 , pp. 178-188
    • Dorgai, L.1    Yagil, E.2    Weisberg, R.A.3
  • 15
    • 0028584269 scopus 로고
    • Crystal structure of the catalytic domain of HIV-1 integrase: Similarity to other polynucleotidyl transferases
    • Dyda F., Hickman A.B., Jenkins T.M., Engelman A., Craigie R., Davies D.R. Crystal structure of the catalytic domain of HIV-1 integrase Similarity to other polynucleotidyl transferases. Science. 266:1994;1981-1986
    • (1994) Science , vol.266 , pp. 1981-1986
    • Dyda, F.1    Hickman, A.B.2    Jenkins, T.M.3    Engelman, A.4    Craigie, R.5    Davies, D.R.6
  • 17
    • 0030816550 scopus 로고    scopus 로고
    • The integrase family of tyrosine recombinases: Evolution of a conserved active site domain
    • Esposito D., Scocca J.J. The integrase family of tyrosine recombinases evolution of a conserved active site domain. Nucl. Acids Res. 25:1997;3605-3614
    • (1997) Nucl. Acids Res. , vol.25 , pp. 3605-3614
    • Esposito, D.1    Scocca, J.J.2
  • 18
    • 0026717832 scopus 로고
    • Mutagenesis of a conserved region of the gene, encoding the FLP recombinase of Saccharomyces cerevisiae
    • Friesen H., Sadowski P.D. Mutagenesis of a conserved region of the gene, encoding the FLP recombinase of Saccharomyces cerevisiae. J. Mol. Biol. 225:1992;313-326
    • (1992) J. Mol. Biol. , vol.225 , pp. 313-326
    • Friesen, H.1    Sadowski, P.D.2
  • 19
    • 0021014246 scopus 로고
    • Overexpression and purification of the sigma subunit of Escherichia coli RNA polymerase
    • Gribskov M., Burgess R.R. Overexpression and purification of the sigma subunit of Escherichia coli RNA polymerase. Gene. 26:1983;109-118
    • (1983) Gene , vol.26 , pp. 109-118
    • Gribskov, M.1    Burgess, R.R.2
  • 20
    • 0030886293 scopus 로고    scopus 로고
    • Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse
    • Guo F., Gopaul D.N., Van Duyne G.D. Structure of Cre recombinase complexed with DNA in a site-specific recombination synapse. Nature. 389:1997;40-46
    • (1997) Nature , vol.389 , pp. 40-46
    • Guo, F.1    Gopaul, D.N.2    Van Duyne, G.D.3
  • 21
    • 0028125987 scopus 로고
    • Mapping the functional domains of bacteriophage lambda integrase protein
    • Han Y.W., Gumport R.I., Gardner J.F. Mapping the functional domains of bacteriophage lambda integrase protein. J. Mol. Biol. 235:1994;908-925
    • (1994) J. Mol. Biol. , vol.235 , pp. 908-925
    • Han, Y.W.1    Gumport, R.I.2    Gardner, J.F.3
  • 22
    • 0030904786 scopus 로고    scopus 로고
    • Molecular organization in site-specific recombination: The catalytic domain of bacteriophage HP1 integrase at 2.7 Å resolution
    • Hickman A.B., Waninger S., Scocca J.J., Dyda F. Molecular organization in site-specific recombination The catalytic domain of bacteriophage HP1 integrase at 2.7 Å resolution. Cell. 89:1997;227-237
    • (1997) Cell , vol.89 , pp. 227-237
    • Hickman, A.B.1    Waninger, S.2    Scocca, J.J.3    Dyda, F.4
  • 23
    • 0025600971 scopus 로고
    • DNA specificity of the Cre recombinase resides in the 25 kDa carboxyl domain of the protein
    • Hoess R., Abremski K., Irwin S., Kendall M., Mack A. DNA specificity of the Cre recombinase resides in the 25 kDa carboxyl domain of the protein. J. Mol. Biol. 216:1990;873-882
    • (1990) J. Mol. Biol. , vol.216 , pp. 873-882
    • Hoess, R.1    Abremski, K.2    Irwin, S.3    Kendall, M.4    MacK, A.5
  • 24
    • 0018070654 scopus 로고
    • The bacteriophage λ int gene product
    • Kikuchi Y., Nash H.A. The bacteriophage λ int gene product. J. Biol. Chem. 253:1978;7149-7157
    • (1978) J. Biol. Chem. , vol.253 , pp. 7149-7157
    • Kikuchi, Y.1    Nash, H.A.2
  • 25
    • 0025223119 scopus 로고
    • Mapping of a higher order protein-DNA complex: Two kinds of long-range interactions in λ attL
    • Kim S., Moitoso de Vargas L., Nunes-Düy S.E., Landy A. Mapping of a higher order protein-DNA complex Two kinds of long-range interactions in λ attL. Cell. 63:1990;773-781
    • (1990) Cell , vol.63 , pp. 773-781
    • Kim, S.1    Moitoso De Vargas, L.2    Nunes-Düy, S.E.3    Landy, A.4
  • 26
    • 0022731677 scopus 로고
    • Two regulatory fim genes, fimB and fimE, control the phase variation of type 1 fimbriae in Escherichia coli
    • Klemm P. Two regulatory fim genes, fimB and fimE, control the phase variation of type 1 fimbriae in Escherichia coli. EMBO J. 5:1986;1389-1393
    • (1986) EMBO J. , vol.5 , pp. 1389-1393
    • Klemm, P.1
  • 27
    • 0001656001 scopus 로고    scopus 로고
    • Flexibility in DNA recombination: Structure of the λ integrase catalytic core
    • Kwon H.J., Tirumalai R.S., Landy A., Ellenberger T. Flexibility in DNA recombination Structure of the λ integrase catalytic core. Science. 276:1997;126-131
    • (1997) Science , vol.276 , pp. 126-131
    • Kwon, H.J.1    Tirumalai, R.S.2    Landy, A.3    Ellenberger, T.4
  • 28
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:1970;680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 29
    • 0027435209 scopus 로고
    • Mechanistic and structural complexity in the site-specific recombination pathways of Int and FLP
    • Landy A. Mechanistic and structural complexity in the site-specific recombination pathways of Int and FLP. Curr. Opin. Genet. Dev. 3:1993;699-707
    • (1993) Curr. Opin. Genet. Dev. , vol.3 , pp. 699-707
    • Landy, A.1
  • 30
    • 0021714343 scopus 로고
    • Purification and properties of Int-H, a variant protein involved in site-specific recombination of bacteriophage λ
    • Lange-Gustafson B.J., Nash H.A. Purification and properties of Int-H, a variant protein involved in site-specific recombination of bacteriophage λ J. Biol. Chem. 259:1984;12724-12732
    • (1984) J. Biol. Chem. , vol.259 , pp. 12724-12732
    • Lange-Gustafson, B.J.1    Nash, H.A.2
  • 31
    • 0021659887 scopus 로고
    • Site-specific recombination systems of phages φ80 and P22: Binding sites of integration host factor and recombination-induced mutations
    • Leong J.M., Nunes-Düby S., Oser A., Youderian P., Susskind M.M., Landy A. Site-specific recombination systems of phages φ80 and P22 binding sites of integration host factor and recombination-induced mutations. Cold Spring Harbor Symp. Quant. Biol. 49:1984;707-714
    • (1984) Cold Spring Harbor Symp. Quant. Biol. , vol.49 , pp. 707-714
    • Leong, J.M.1    Nunes-Düby, S.2    Oser, A.3    Youderian, P.4    Susskind, M.M.5    Landy, A.6
  • 32
    • 0029971048 scopus 로고    scopus 로고
    • Genetic analysis of the bacteriophage λ attL nucleoprotein complex
    • MacWilliams M.P., Gumport R.I., Gardner J.F. Genetic analysis of the bacteriophage λ attL nucleoprotein complex. Genetics. 143:1996;1069-1079
    • (1996) Genetics , vol.143 , pp. 1069-1079
    • MacWilliams, M.P.1    Gumport, R.I.2    Gardner, J.F.3
  • 33
    • 0016589998 scopus 로고
    • Inactivation of rat liver RNA polymerases I and II and yeast RNA polymerase I by pyridoxal 5′-phosphate. Evidence for the participation of lysyl residues at the active site
    • Martial J., Zaldivar J., Bull P., Venegas A., Valenzuela P. Inactivation of rat liver RNA polymerases I and II and yeast RNA polymerase I by pyridoxal 5′-phosphate. Evidence for the participation of lysyl residues at the active site. Biochemistry. 14:1975;4907-4911
    • (1975) Biochemistry , vol.14 , pp. 4907-4911
    • Martial, J.1    Zaldivar, J.2    Bull, P.3    Venegas, A.4    Valenzuela, P.5
  • 34
    • 0024295418 scopus 로고
    • Autonomous DNA binding domains of λ integrase recognize different sequence families
    • Moitoso de Vargas L., Pargellis C.A., Hasan N.M., Bushman E.W., Landy A. Autonomous DNA binding domains of λ integrase recognize different sequence families. Cell. 54:1988;923-929
    • (1988) Cell , vol.54 , pp. 923-929
    • Moitoso De Vargas, L.1    Pargellis, C.A.2    Hasan, N.M.3    Bushman, E.W.4    Landy, A.5
  • 35
    • 0024340762 scopus 로고
    • DNA looping generated by the DNA-bending protein IHF and the two domains of λ integrase
    • Moitoso de Vargas L., Kim S., Landy A. DNA looping generated by the DNA-bending protein IHF and the two domains of λ integrase. Science. 244:1989;1457-1461
    • (1989) Science , vol.244 , pp. 1457-1461
    • Moitoso De Vargas, L.1    Kim, S.2    Landy, A.3
  • 36
    • 0000078911 scopus 로고    scopus 로고
    • Site-specific recombination: Integration, excision, resolution, and inversion of defined DNA segments
    • F.C., Neidhardt, R. III Curtiss, J.L., Ingraham, E.C.C., Lin, K.B., Low, B. Magasanik, W.S. Reznikoff, M. Riley, M. Schaechter, & H.E. Umbarger. Washington: ASM Press
    • Nash H.A. Site-specific recombination Integration, excision, resolution, and inversion of defined DNA segments. Neidhardt F.C., Curtiss R. III, Ingraham J.L., Lin E.C.C., Low K.B., Magasanik B., Reznikoff W.S., Riley M., Schaechter M., Umbarger H.E. Escherichia coli and Salmonella. 1996;2363-2376 ASM Press, Washington
    • (1996) Escherichia Coli and Salmonella , pp. 2363-2376
    • Nash, H.A.1
  • 37
    • 0023667024 scopus 로고
    • Site-specific recombination intermediates trapped with suicide substrates
    • Nunes-Düby S.E., Matsumoto L., Landy A. Site-specific recombination intermediates trapped with suicide substrates. Cell. 50:1987;779-788
    • (1987) Cell , vol.50 , pp. 779-788
    • Nunes-Düby, S.E.1    Matsumoto, L.2    Landy, A.3
  • 38
    • 0038659759 scopus 로고    scopus 로고
    • Similarities and differences among 105 members of the Int family of site-specific recombinases
    • Nunes-Düby S., Tirumalai R.S., Kwon H.J., Ellenberger T., Landy A. Similarities and differences among 105 members of the Int family of site-specific recombinases. Nucl. Acids Res. 26:1998;391-406
    • (1998) Nucl. Acids Res. , vol.26 , pp. 391-406
    • Nunes-Düby, S.1    Tirumalai, R.S.2    Kwon, H.J.3    Ellenberger, T.4    Landy, A.5
  • 39
    • 0027159168 scopus 로고
    • Mechanism of cleavage and ligation by the FLP recombinase: Classification of mutations in the FLP protein using in vitro complementation analysis
    • Pan G., Luetke K., Sadowski P.D. Mechanism of cleavage and ligation by the FLP recombinase Classification of mutations in the FLP protein using in vitro complementation analysis. Mol. Cell. Biol. 13:1993;3167-3175
    • (1993) Mol. Cell. Biol. , vol.13 , pp. 3167-3175
    • Pan, G.1    Luetke, K.2    Sadowski, P.D.3
  • 40
    • 0028177608 scopus 로고
    • 2- and COOH- terminal domains of the FLP recombinase with the FLP recognition target sequence
    • 2- and COOH- terminal domains of the FLP recombinase with the FLP recognition target sequence. J. Biol. Chem. 269:1994;10940-10945
    • (1994) J. Biol. Chem. , vol.269 , pp. 10940-10945
    • Panigrahi, G.B.1    Sadowski, P.D.2
  • 41
    • 0024278670 scopus 로고
    • Suicide recombination substrates yield covalent λ integrase-DNA complexes and lead to identification of the active site tyrosine
    • Pargellis C.A., Nunes-Düby S.E., Moitoso de Vargas L., Landy A. Suicide recombination substrates yield covalent λ integrase-DNA complexes and lead to identification of the active site tyrosine. J. Biol. Chem. 263:1988;7678-7685
    • (1988) J. Biol. Chem. , vol.263 , pp. 7678-7685
    • Pargellis, C.A.1    Nunes-Düby, S.E.2    Moitoso De Vargas, L.3    Landy, A.4
  • 42
    • 0023708318 scopus 로고
    • Step-arrest mutants of FLP recombinase: Implications for the catalytic mechanism of DNA recombination
    • Parsons R.L., Prasad P.V., Harshey R.M., Jayaram M. Step-arrest mutants of FLP recombinase Implications for the catalytic mechanism of DNA recombination. Mol. Cell. Biol. 8:1988;3303-3310
    • (1988) Mol. Cell. Biol. , vol.8 , pp. 3303-3310
    • Parsons, R.L.1    Prasad, P.V.2    Harshey, R.M.3    Jayaram, M.4
  • 43
    • 0023854278 scopus 로고
    • Synapsis of attachment sites during lambda integrative recombination involves capture of a naked DNA by a protein-DNA complex
    • Richet E., Abcarian P., Nash H.A. Synapsis of attachment sites during lambda integrative recombination involves capture of a naked DNA by a protein-DNA complex. Cell. 52:1988;9-17
    • (1988) Cell , vol.52 , pp. 9-17
    • Richet, E.1    Abcarian, P.2    Nash, H.A.3
  • 44
    • 0018691250 scopus 로고
    • Interaction of Int protein with specific sites on λ attDNA
    • Ross W., Landy A., Kikuchi Y., Nash H. Interaction of Int protein with specific sites on λ attDNA. Cell. 18:1979;297-307
    • (1979) Cell , vol.18 , pp. 297-307
    • Ross, W.1    Landy, A.2    Kikuchi, Y.3    Nash, H.4
  • 45
    • 0027173542 scopus 로고
    • Site-specific genetic recombination: Hops, flips and flops
    • Sadowski P.D. Site-specific genetic recombination hops, flips and flops. FASEB. 7:1993;760-767
    • (1993) FASEB , vol.7 , pp. 760-767
    • Sadowski, P.D.1
  • 48
  • 50
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189:1986;113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 52
    • 0021919826 scopus 로고
    • A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes
    • Tabor S., Richardson C.C. A bacteriophage T7 RNA polymerase/promoter system for controlled exclusive expression of specific genes. Proc. Natl Acad. Sci. USA. 82:1985;1074-1078
    • (1985) Proc. Natl Acad. Sci. USA , vol.82 , pp. 1074-1078
    • Tabor, S.1    Richardson, C.C.2
  • 53
    • 0025690281 scopus 로고
    • Characterization of the ATP binding site on Escherichia coli DNA gyrase
    • Tamura J.K., Gellert M. Characterization of the ATP binding site on Escherichia coli DNA gyrase. J. Biol. Chem. 265:1990;21342-21349
    • (1990) J. Biol. Chem. , vol.265 , pp. 21342-21349
    • Tamura, J.K.1    Gellert, M.2
  • 55
    • 0023660545 scopus 로고
    • A mutational analysis of the bacteriophage P1 recombinase Cre
    • Wierzbicki A., Kendall M., Abremski K., Hoess R. A mutational analysis of the bacteriophage P1 recombinase Cre. J. Mol. Biol. 195:1987;785-794
    • (1987) J. Mol. Biol. , vol.195 , pp. 785-794
    • Wierzbicki, A.1    Kendall, M.2    Abremski, K.3    Hoess, R.4
  • 56
    • 0026323541 scopus 로고
    • Identification of amino acid residues at interface of protein-nucleic acid complexes by photochemical cross-linking
    • Williams K.R., Konigsberg W.H. Identification of amino acid residues at interface of protein-nucleic acid complexes by photochemical cross-linking. Methods Enzymol. 208:1991;516-539
    • (1991) Methods Enzymol. , vol.208 , pp. 516-539
    • Williams, K.R.1    Konigsberg, W.H.2
  • 57
    • 0029082073 scopus 로고
    • Identifying determinants of recombination specificity: Construction and characterization of chimeric bacteriophage integrases
    • Yagil E., Dorgai L., Weisberg R. Identifying determinants of recombination specificity Construction and characterization of chimeric bacteriophage integrases. J. Mol. Biol. 252:1995;163-177
    • (1995) J. Mol. Biol. , vol.252 , pp. 163-177
    • Yagil, E.1    Dorgai, L.2    Weisberg, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.