Features of the plasmid pMV158-encoded MobM, a protein involved in its mobilization

Journal of Molecular Biology

Volumn 335, Issue 3, 2004, Pages 733-743

  De Antonio, Carmen ^a   Farías, María Eugenia ^a,b   De Lacoba, Mario García ^a   Espinosa, Manuel ^a  

^a CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^b PLANTA PILOTO DE PROCESOS INDUSTRIALES MICROBIOLÓGICOS PROIMI CONICET   (Argentina)

Author keywords

CD, circular dichroism; DNA relaxase; Homology modelling; Membrane associated protein; Plasmid mobilization protein; Pre Mob proteins; Tm, melting temperature

Indexed keywords

DEOXYRIBONUCLEOPROTEIN; BACTERIAL PROTEIN; DEOXYRIBONUCLEASE; MOBM PROTEIN, BACTERIA; PROTEIN SUBUNIT;

ALPHA HELIX; ARTICLE; CELL FRACTIONATION; CIRCULAR DICHROISM; DNA DENATURATION; FLUORESCENCE; GENETIC CODE; HYDROPHOBICITY; MOBILIZATION; MUTATION; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN TRANSPORT; ULTRACENTRIFUGATION; BACTERIUM CONJUGATION; CELL MEMBRANE; CHEMICAL STRUCTURE; CHEMISTRY; DNA SUPERCOILING; GENETICS; METABOLISM; PROTEIN CONFORMATION; PROTEIN DENATURATION; STREPTOCOCCUS; STRUCTURAL HOMOLOGY;

BACTERIA (MICROORGANISMS);

BACTERIAL PROTEINS; CELL MEMBRANE; CONJUGATION, GENETIC; DNA, SUPERHELICAL; ENDODEOXYRIBONUCLEASES; MODELS, MOLECULAR; PLASMIDS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN SUBUNITS; PROTEIN TRANSPORT; STREPTOCOCCUS; STRUCTURAL HOMOLOGY, PROTEIN;

EID: 1542711638     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2003.11.017     Document Type: Article

References (49)

1. Thomas C.M. The Horizontal Gene Pool. 2000;Harwood Academic Publishers, Amsterdam.
2. Lanka E., Wilkins B.M. DNA processing reactions in bacterial conjugation. Annu. Rev. Biochem. 64:1995;141-169.
3. Zechner E.L., de la Cruz F., Eisenbrandt R., Grahn A.M., Koraimann G., Lanka E., et al. Conjugative-DNA transfer processes. Thomas C.M. The Horizontal Gene Pool. 2000;87-174 Harwood Academic publishers, Amsterdam.
4. Byrd D.R., Matson S.W. Nicking by transesterification: the reaction catalyzed by a relaxase. Mol. Microbiol. 25:1997;1011-1022.
5. Pansegrau W., Lanka E. Enzymology of DNA strand transfer by conjugative mechanisms. Prog. Nucl. Acid Res. Mol. Biol. 54:1996;197-251.
6. Moncalián G., Grandoso G., Llosa M., de la Cruz F. OriT-processing and regulatory roles of TrwA protein in plasmid R388 conjugation. J. Mol. Biol. 270:1997;188-200.
7. Grohmann E., Muth G., Espinosa M. Conjugative plasmid transfer in Gram-positive bacteria. Microbiol. Mol. Biol. Rev. 67:2003;277-301.
8. Guzmán L., Espinosa M. The mobilization protein, MobM, of the streptococcal plasmid pMV158 specifically cleaves supercoiled DNA at the plasmid oriT. J. Mol. Biol. 267:1997;688-702.
9. Grohmann E., Guzmán L.M., Espinosa M. Mobilisation of the streptococcal plasmid pMV158: interactions of MobM protein with its cognate oriT DNA region. Mol. Gen. Genet. 261:1999;707-715.
10. Farías M.E., Grohmann E., Espinosa M. Expression of the mobM gene of the streptococcal plasmid pMV158 in Lactococcus lactis subsp. lactis. FEMS Microbiol. Letters. 176:1999;403-410.
11. Farías M.E., Espinosa M. Conjugal transfer of plasmid pMV158: uncoupling of the pMV158 origin of transfer from the mobilization gene mobM, and modulation of pMV158 transfer in Escherichia coli mediated by IncP plasmids. Microbiology. 146:2000;2259-2265.
12. del Solar G., Moscoso M., Espinosa M. Rolling circle-replicating plasmids from Gram-positive and Gram-negative bacteria: a wall falls. Mol. Microbiol. 8:1993;789-796.
13. Varsaki A., Lucas M., Afendra A.S., Drainas C., de la Cruz F. Genetic and biochemical characterization of MbeA, the relaxase involved in plasmid ColE1 conjugative mobilization. Mol. Microbiol. 48:2003;481-493.
14. Pansegrau W., Balzer D., Kruft V., Lanka E. In vitro assembly of relaxosomes at the transfer origin of plasmid RP4. Proc. Natl Acad. Sci. USA. 87:1990;6555-6559.
15. Llosa M., Grandoso G., de la Cruz F. Nicking activity of TrwC directed against the origin of transfer of the IncW plasmid R388. J. Mol. Biol. 246:1995;54-62.
16. Matson S.W., Morton B.S. Escherichia coli DNA helicase I catalyzes a site- and strand-specific nicking reaction at the F plasmid oriT. J. Biol. Chem. 266:1991;16232-16237.
17. Pace C.N., Vajdos F., Fee L., Grimsley G., Gray T. How to measure and predict the molar absorption coefficient of a protein. Protein Sci. 4:1995;2411-2423.
18. Philo J. An improved function for fitting sedimentation velocity data for low-molecular weight solutes. Biophys. J. 72:1997;435-444.
19. Park K., Perczel A., Fassman G.D. Differentiation between transmembrane helices and peripheral helices by the deconvolution of circular dichroism spectra of membrane proteins. Protein Sci. 1:1992;1032-1049.
20. Garnier J., Gibrat J.F., Robson B. GOR secondary structure prediction method version IV. Methods Enzymol. 266:1996;540-553.
21. Geourjon C., Deléage G. Significant improvement in protein secondary structure prediction by consensus prediction from multiple alignments. Cabios. 11:1995;681-684.
22. Lupas A., van Dyke M., Stock J. Predicting coiled coils from protein sequences. Science. 252:1991;1162-1164.
23. Berger B., Wilson D.B., Wolf E., Tonchev T., Milla M., Kim P.S. Predicting coiled coils by use of pairwise residue correlations. Proc. Natl Acad. Sci. USA. 92:1995;8259-8263.
24. Grahn A.M., Haase J., Bamford D.H., Lanka E. Components of the RP4 conjugative transfer apparatus form an envelope structure bridging inner and outer membranes of donor cells: implications for related macromolecule transport systems. J. Bacteriol. 182:2000;1564-1574.
25. Bravo A., Salas M. Initiation of bacteriophage φ29 DNA replication in vivo: assembly of a membrane-associated multiprotein complex. J. Mol. Biol. 269:1997;102-112.
26. Gomis-Rüth F.X., Moncalián G., de la Cruz F., Coll M. Conjugative plasmid protein TrwB, an integral membrane tipe IV secretion system coupling protein. Detailed structural features and mapping of the active site cleft. J. Biol. Chem. 277:2002;7556-7566.
27. Kosono S., Kataoka M., Seki T., Yoshida T. The TraB protein, which mediates the intermycelial transfer of the Streptomyces plasmid pSN22, has functional NTP-binding motifs and is localized to the cytoplasmic membrane. Mol. Microbiol. 19:1996;397-405.
28. Koonin E.V., Ilyina T.W. Computer-assisted dissection of rolling circle DNA replication. BioSystems. 30:1993;241-268.
29. Pansegrau W., Lanka E. Common sequence motifs in DNA relaxases and nick regions from a variety of DNA transfer systems. Nucl. Acids Res. 19:1991;3455.
30. Wiener M., Freymann D., Ghosh P., Stroud R.M. Crystal structure of colicin Ia. Nature. 385:1997;461-464.
31. Bowie J.U., Luthy R., Eisenberg D. A method to identify protein sequences that fold into a known three-dimensional structure. Science. 253:1991;164-170.
32. Grohmann E., Zechner E.L., Espinosa M. Determination of specific DNA strand discontinuities with nucleotide resolution in exponentially growing bacteria harbouring rolling circle-replicating plasmids. FEMS Microbiol. Letters. 152:1997;363-369.
33. Wang P., Projan S.J., Henriquez V., Novick R.P. Origin recognition specificity in pT181 plasmids is determined by a functionally asymmetric palindrome DNA-element. EMBO J. 12:1993;45-52.
34. Studier F.W., Rosenberg A.H., Dunn J.J., Dubendorff J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185:1990;60-89.
35. del Solar G., Díaz R., Espinosa M. Replication of the streptococcal plasmid pMV158 and derivatives in cell-free extracts of Escherichia coli. Mol. Gen. Genet. 206:1987;428-435.
36. Higuchi R. Recombinant PCR. PCR Protocols: A Guide to Methods and Applications. 1990;Academic Press, New York.
37. Acebo P., Garcia de Lacoba M., Rivas G., Andreu J.M., Espinosa M., del Solar G. Structural features of the plasmid pMV158-encoded transcriptional repressor CopG, a protein sharing similarities with both helix-turn-helix and β-sheet DNA binding proteins. Proteins: Struct. Funct. Genet. 32:1998;248-261.
38. Siegel L.M., Monty K.J. Determination of molecular weights and frictional ratios of proteins in impure systems by the use of gel filtration and density gradient centrifugation. Applications to crude preparations of sulfite and hydroxylamine reductases. Biochem. Biophys. Acta. 112:1966;346-362.
39. Minton A.P. Conservation of signal: a new algorithm for the elimination of the reference concentration as an independently variable parameter in the analysis of sedimentation equilibrium. Schuster T.M., Laue T.M. Modern Analytical Ultracentrifugation. 1994;81-93 Birckhouser, Boston.
40. Laue T.M., Shah B.D., Ridgeway T.M., Pelletier S.L. Computer-aided interpretation of analytical sedimentation data for proteins. Harding S.E., Rowe A., Horton J.C. Analytical Ultracentrifugation in Biochemistry and Polymer Sciences. 1992;90-125 Royal Society of Chemistry, Cambridge.
41. Schuck P., Rossmanith P. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers. 54:2000;328-341.
42. van Holde K.E. Hall E.C.P. Physical Biochemistry. 1985.
43. Pessen H., Kumosinsky T.F. Measurement of protein hydration by various techniques. Methods Enzymol. 117:1985;219-255.
44. Sreerama N., Woody R.W. Estimation of protein secondary structure from CD spectra: comparison of CONTIN, SELCON and CDSSTR methods with an expanded reference set. Anal. Biochem. 287:2000;252-260.
45. Perczel A., Park K., Fasman G.D. Decon volution of the circular dichroism spectra of proteins: the circular dichroism spectra of the antiparallel β-sheet in proteins. Proteins: Struct. Funct. Genet. 13:1992;57-69.
46. Andrade M.A., Chacón P., Merolo J.J., Morán F. Evaluation of secondary structure of proteins from UV circular dichroism spectra using an unsupervised learning neural network. Protein Eng. 6:1993;443-454.
47. Perczel A., Park K., Fassman G.D. Analysis of the circular dichroism spectrum of proteins using the convex constraint algorithm: a practical guide. Anal. Biochem. 203:1992;83-93.
48. Kelley L.A., MacCallum R.M., Sternberg M.J.E. Enhanced genome annotation using structural profiles into the program 3D-PSSM. J. Mol. Biol. 299:2000;499-520.
49. Rost B., Schenider R., Sander C. Protein fold recognition by prediction-based threading. J. Mol. Biol. 270:1997;471-480.