Characterization of the interaction between the restriction endonuclease McrBC from E. coli and its cofactor GTP

Journal of Molecular Biology

Volumn 272, Issue 2, 1997, Pages 190-199

  Pieper, Uwe ^a   Brinkmann, Thilo ^a   Krüger, Torsten ^b   Noyer Weidner, Mario ^b   Pingoud, Alfred ^a  

^a JUSTUS LIEBIG UNIVERSITY   (Germany)

^b MAX PLANCK INSTITUTE FOR MOLECULAR GENETICS   (Germany)

Author keywords

5 methylcytosine; DNA modification; GTP hydrolysis; GTPase; Restriction enzymes

Indexed keywords

BACTERIAL ENZYME; GUANINE NUCLEOTIDE; GUANINE NUCLEOTIDE BINDING PROTEIN; GUANOSINE DIPHOSPHATE; GUANOSINE TRIPHOSPHATE; MAGNESIUM ION; PROTEIN SUBUNIT; RESTRICTION ENDONUCLEASE;

ARTICLE; BINDING AFFINITY; CHEMICAL REACTION KINETICS; CONSENSUS SEQUENCE; CONTROLLED STUDY; DNA CLEAVAGE; DRUG HYDROLYSIS; ENZYME ACTIVITY; ENZYME STABILITY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN DNA BINDING; PROTEIN INTERACTION;

BACTERIA (MICROORGANISMS);

EID: 0030829590     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1006/jmbi.1997.1228     Document Type: Article

References (37)

1. Bickle T. The ATP-dependent restriction enzymes. Nucleases. 1993;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
2. 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.
3. Carlier M. F., Pantaloni D. Tubulin as a G-protein: regulation of tubulin-tubulin interactions by GTP hydrolysis. Bosch L., Kraal B., Parmeggiani A. The Guanine-Nucleotide Binding Proteins. 1989;Plenum Press, New York and London.
4. Dever T. E., Glynias M. J., Merrick W. C. GTP-binding domain: three consensus sequence elements with distinct spacing. Proc. Natl Acad. Sci. USA. 84:1987;1814-1818.
5. Didsbury J., Weber R. F., Bokoch G. M., Evans T., Snyderman R. Rac, a novel ras related family of proteins that are botulinum toxin substrates. J. Biol. Chem. 264:1989;16378-16382.
6. Dila D., Sutherland E., Moran L., Slatko B., Raleigh E. A. Genetic and sequence organization of the mcrBC locus of Escherichia coli K-12. J. Bacteriol. 172:1990;4888-4900.
7. Feuerstein J., Goody R. S., Wittinghofer A. Preparation and characterization of nucleotide-free and metal ion-free p21 "apoprotein" J. Biol. Chem. 262:1987;8455-8458.
8. Forchhammer K., Leinfelder W., Böck A. Identification of a novel translation factor necessary for the incorporation of selenocysteine into protein. Nature. 342:1989;453-456.
9. Gideon P., John J., Frech M., Lautwein A., Clark R., Scheffler J. E., Wittinghofer A. Mutational and kinetic analyses of the GTPase-activating protein (GAP)-p21 interaction: the C-terminal domain of GAP is not sufficient for full activity. Mol. Cell. Biol. 12:1992;2050-2056.
10. Heitman J., Model P. Site-specific methylases induce the SOS DNA repair response in Escherichia coli. J. Bacteriol. 169:1987;3243-3250.
11. Hwang Y. W., Miller D. L. A mutation that alters the nucleotide specificity of elongation factor Tu, a GTP regulatory protein. J. Biol. Chem. 262:1987;13081-13085.
12. Ito W., Ishiguro H., Kurosawa Y. A general method for introducing a series of mutations into cloned DNA using the polymerase chain reaction. Gene. 102:1991;67-70.
13. Jensen M., Cool R. H., Mortensen K. K., Clark B. F. C., Parmeggiani A. Structure-function relationships of elongation factor Tu. Eur. J. Biochem. 182:1989;247-255.
14. Kelleher J. E., Raleigh E. A. A novel activity in Escherichia coli K-12 that directs restriction of DNA modified at CG dinucleotides. J. Bacteriol. 173:1991;5520-5523.
15. Kjeldgaard M., Nyborg J., Clark B. F. C. The GTP binding motif: variations on a theme. FASEB J. 10:1996;1347-1368.
16. Krüger, T. 1992, Überproduktion, Reinigung und Charakterisierung der Untereinheiten des McrBC-Restriktionssystems von Escherichia coli K-12. Ph.D. thesis, Freie Universität, Berlin.
17. Krüger T., Grund C., Wild C., Noyer-Weidner M. Characterization of the mcrBC region of Escherichia coli K-12 wild-type and mutant strains. Gene. 114:1992;1-12.
18. Krüger T., Wild C., Noyer-Weidner M. McrB: a prokaryotic protein specifically recognizing DNA containing modified cytosine residues. EMBO J. 14:1995;2661-2669.
19. Lucas-Lenard J., Lipmann F. Separation of three microbial amino acid polymerization factors. Proc. Natl Acad. Sci. USA. 55:1966;1562-1566.
20. Luria S. E., Human M. L. A nonhereditary, host-induced variation of bacterial viruses. J. Bacteriol. 64:1952;557-559.
21. Miller D. L., Weissbach H. Elongation factor Tu and the aminoacyl-tRNA·EFTu·GTP complex. Methods Enzymol. 30:1974;219-232.
22. Nock S., Grillenbeck N., Ahmadian M. R., Ribeiro S., Kreutzer R., Sprinzl M. Properties of isolated domains of the elongation factor Tu from Thermus thermophilus HB8. Eur. J. Biochem. 234:1995;132-139.
23. Noyer-Weidner M., Trautner T. A. Methylation of DNA in prokaryotes. Jost J. P., Saluz H. D. DNA Methylation: Molecular Biology and Biological Significance. 1993;Birkhäuser Verlag, Basel.
24. Noyer-Weidner M., Diaz R., Reiners L. Cytosine-specific DNA modification interfers with plasmid establishment in Escherichia coli K12: Involvement of rgl B. Mol. Gen. Genet. 205:1986;469-475.
25. O'Sullivan D. J., Zagula K., Klaenhammer T. R. In vivo restriction by LlaI is encoded by three genes, arranged in an operon with llaIM, on the conjugative Lactococcus plasmid pTR2030. J. Bacteriol. 177:1995;134-143.
26. Parmeggiani A., Swart G. W. M., Mortensen K., Jensen J., Clark B. F. C., Dente L., Cortese R. Properties of a genetically engineered G domain of elongation factor Tu. Proc. Natl Acad. Sci. USA. 84:1987;3141-3145.
27. Pingoud A., Jeltsch A. Recognition and cleavage of DNA by type II restriction endonucleases. Eur. J. Biochem. 246:1997;1-22.
28. Pingoud A., Urbanke C., Krauss G., Peters F., Maass G. Ternary complex formation between elongation factor Tu, GTP and aminoacyl-tRNA: an equilibrium study. Eur. J. Biochem. 78:1977;403-409.
29. Pingoud A., Pieper U., Busche R., Ehbrecht H.-J., Wehrmann M., Gast F.-U., Feuerstein J., Wittinghofer A., Jarchau T., Koring G.-W., Mayer F. Structural and functional studies on c-p21, v-p21 and the genetically engineered guanine nucleotide binding domain of EF-Tu. Bosch L., Kraal B., Parmeggiani A. The Guanine-Nucleotide Binding Proteins. 1989;Plenum Press, New York and London.
30. Raleigh E., Wilson G. Escherichia coli K-12 restricts DNA containing 5-methylcytosine. Proc. Natl Acad. Sci. USA. 83:1986;9070-9074.
31. Raleigh E. A., Trimarchi R., Revel H. Genetic and physical mapping of the mcrA (rglA) and mcrB (rglB) loci of Escherichia coli K-12. Genetics. 122:1989;279-296.
32. Revel H. R. DNA modification: glucosylation. Mathews C. K., Kutter E. M., Mosig G., Berget G. Bacteriophage T4. 1983;American Society for Microbiology, Washington.
33. Roberts R. J., Halford S. E. Type II restriction endonucleases. Linn S. M., Lloyd R. R., Roberts R. J. Nucleases. 1993;Cold Spring Harbor Laboratory Press, Cold Spring Harbor.
34. Ross T. R., Achberger E. C., Braymer H. D. Nucleotide sequence of the McrB region of Escherichia coli K-12 and evidence for two independent translational initiation sites at the mcrB locus. J. Bacteriol. 171:1989;1974-1981.
35. Sutherland E., Coe L., Raleigh E. A. McrBC: a multisubunit GTP-dependent restriction endonuclease. J. Mol. Biol. 225:1992;327-348.
36. Webb J. L., King G., Ternent D., Titheradge A. J., Murray N. E. Restriction by EcoKI is enhanced by co-operative interactions between target sequences and is dependent on DEAD box motifs. EMBO J. 15:1996;2003-2009.
37. Wittinghofer A., Leberman R. Elongation factor T from Bacillus stearothermophilus and Escherichia coli. Purification and some properties of EF-Tu and EF-Ts from Bacillus stearothermophilus. Eur. J. Biochem. 62:1976;373-382.