Structural features of the initiator of replication protein RepB encoded by the promiscuous plasmid pMV158

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1696, Issue 1, 2004, Pages 113-119

  Ruiz Masó, José A ^a   López Zumel, Consuelo ^b   Menéndez, Margarita ^b   Espinosa, Manuel ^a   Del Solar, Gloria ^a  

^a CENTRO DE INVESTIGACIONES BIOLÓGICAS   (Spain)

^b INSTITUTO DE QUÍMICA FÍSICA ROCASOLANO   (Spain)

Author keywords

Analytical ultracentrifugation; Circular dichroism; Conformational change; Initiator of replication protein

Indexed keywords

DNA; DNA TOPOISOMERASE; HELICASE;

ALPHA HELIX; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME STRUCTURE; ESCHERICHIA COLI; NONHUMAN; PLASMID; PRIORITY JOURNAL; PROTEIN PURIFICATION; PROTEIN STRUCTURE; TEMPERATURE DEPENDENCE; ULTRACENTRIFUGATION;

EID: 1242351589     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.09.010     Document Type: Article

References (31)

1. del Solar G., Giraldo R., Ruiz-Echevarría M.J., Espinosa M., Díaz-Orejas R. Replication and control of circular bacterial plasmids. Microbiol. Mol. Biol. Rev. 62:1998;434-464.
2. Khan S.A. Rolling-circle replication of bacterial plasmids. Microbiol. Mol. Biol. Rev. 61:1997;442-455.
3. Khan S.A. Plasmid rolling-circle replication: recent developments. Mol. Microbiol. 37:2000;477-484.
4. Rasooly A., Novick R.P. Replication-specific inactivation of the pT181 plasmid initiator protein. Science. 262:1993;1048-1050.
5. Kramer M.G., Khan S.A., Espinosa M. Plasmid rolling circle replication: identification of the RNA polymerase-directed primer RNA and requirement of DNA polymerase I for lagging strand initiation. EMBO J. 16:1997;5784-5795.
6. Dempsey L.A., Birch P., Khan S.A. Six amino acids determine the sequence-specific DNA binding and replication specificity of the initiator proteins of the pT181 family. J. Biol. Chem. 267:1992;24538-24543.
7. Jin R., Rasooly A., Novick R.P. In vitro inhibitory activity of RepC/C*, the inactivated form of the pT181 plasmid initiation protein RepC. J. Bacteriol. 179:1997;141-147.
8. Thomas C.D., Balson D.F., Shaw W. Identification of the tyrosine residue involved in bond formation between replication origin and the initiator protein of plasmid pC221. Biochem. Soc. Trans. 16:1990;758-759.
9. de la Campa A.G., del Solar G., Espinosa M. Initiation of replication of plasmid pLS1. The initiator protein RepB acts on two distant DNA regions. J. Mol. Biol. 213:1990;247-262.
10. Moscoso M., Eritja R., Espinosa M. Initiation of replication of plasmid pMV158: mechanisms of DNA strand transfer reactions mediated by the initiator RepB protein. J. Mol. Biol. 268:1997;840-856.
11. Moscoso M., del Solar G., Espinosa M. In vitro recognition of the replication origin of pLS1 and of plasmids of the pLS1 family by the RepB initiator protein. J. Bacteriol. 177:1995;7041-7049.
12. 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.
13. 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.
14. 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.
15. Schuck P., Rossmanith P. Determination of the sedimentation coefficient distribution by least-squares boundary modeling. Biopolymers. 54:2000;328-341.
16. van Holde K.E. Physical Biochemistry. 1985;Prentice-Hall, Englewood Cliffs.
17. Pessen H., Kumosinsky T.F. Measurement of protein hydration by various techniques. Methods Enzymol. 117:1985;219-255.
18. Provencher S.W., Glockner J. Estimation of globular protein secondary structure from circular dichroism. Biochemistry. 20:1981;33-37.
19. 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.
20. Böhm G., Muhr R., Jaenicke R. Quantitative analysis of protein far UV circular dichroism spectra by neural networks. Protein Eng. 5:1992;191-195.
21. Rost B., Sander C. Combining evolutionary information and neural networks to predict protein secondary structure. Proteins: Struct. Funct. Genet. 19:1994;55-72.
22. Rost B. J. protein secondary structure prediction continues to rise. Struct. Biol. 134:2001;204-218.
23. McGuffin B.K., Jones D.T. The PSIPRED protein structure prediction server. Bioinformatics. 16:2000;404-405.
24. Eyrich V.A., Marti-Renom M.A., Przbylski D., Madhusudhan M.S., Fiser A., Pazos F., Valencia A., Sali A., Rost B. EVA: continuous automatic evaluation of protein structure prediction servers. Bioinformatics. 17:2001;1242-1243.
25. Hofmann K., Brucher P., Falquet L., Bairoch A. The PROSITE database, its status in 1999. Nucleic Acids Res. 27:1999;215-219.
26. 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.
27. Priebe S.D., Lacks S.A. Region of the streptococcal plasmid pMV158 required for conjugative mobilization. J. Bacteriol. 171:1989;4778-4784.
28. del Solar G., Acebo P., Espinosa M. Replication control of plasmid pLS1: efficient regulation of plasmid copy number is exerted by the combined action of two plasmid components, CopG and RNA II. Mol. Microbiol. 18:1995;913-924.
29. García de Viedma D., Giraldo R., Rivas G., Fernández- Tresguerres E., Díaz-Orejas R. A leucine zipper motif determines different functions in a DNA replication protein. EMBO J. 15:1996;925-934.
30. Wang P., Projan S.J., Henriquez V., Novick R.P. Specificity of origin recognition by replication initiator protein in plasmids of the pT181 family is determined by six amino acid residues element. J. Mol. Biol. 223:1992;145-158.
31. Moscoso M., del Solar G., Espinosa M. Specific nicking-closing activity of the initiator of replication protein RepB of plasmid pMV158 on supercoiled or single-stranded DNA. J. Biol. Chem. 270:1995;3772-3779.