Purification and functional analysis of recombinant Acholeplasma laidlawii histone-like HU protein

Biochimie

Volumn 93, Issue 7, 2011, Pages 1102-1109

  Levitskiy, S A ^a,b   Sycheva, A M ^c   Kharlampieva, D D ^a   Oberto, J ^d   Kamashev, D E ^a,b   Serebryakova, M V ^a   Moshkovskii, S A ^c   Lazarev, V N ^a,b   Govorun, V M ^a,b  

^a FEDERAL RESEARCH AND CLINICAL CENTER OF PHYSICAL CHEMICAL MEDICINE OF FEDERAL MEDICAL BIOLOGICAL AGENCY   (Russian Federation)

^b KURCHATOV INSTITUTE   (Russian Federation)

^c INSTITUTE OF BIOMEDICAL CHEMISTRY   (Russian Federation)

^d UNIVERSITÉ PARIS SACLAY   (France)

Author keywords

Acholeplasma laidlawii; Histone like protein; HU protein; SPR

Indexed keywords

BACTERIAL PROTEIN; HOMODIMER; HU PROTEIN; NUCLEASE; RECOMBINANT PROTEIN;

ACHOLEPLASMA LAIDLAWII; ARTICLE; BACTERIAL GENE; BACTERIAL GROWTH; BACTERIAL STRAIN; CONTROLLED STUDY; DNA BINDING; ENZYME ACTIVITY; ESCHERICHIA COLI; GENE EXPRESSION; NONHUMAN; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN PURIFICATION; WILD TYPE;

ACHOLEPLASMA LAIDLAWII; BACTERIAL PROTEINS; DNA; DNA, CIRCULAR; DNA, SUPERHELICAL; DNA-BINDING PROTEINS; ELECTROPHORESIS, POLYACRYLAMIDE GEL; ESCHERICHIA COLI; GENETIC COMPLEMENTATION TEST; MUTATION; PLASMIDS; PROTEIN BINDING; PROTEIN MULTIMERIZATION; RECOMBINANT PROTEINS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SURFACE PLASMON RESONANCE;

ACHOLEPLASMA LAIDLAWII; ESCHERICHIA COLI;

EID: 79958057464     PISSN: 03009084     EISSN: 61831638     Source Type: Journal    
DOI: 10.1016/j.biochi.2011.03.005     Document Type: Article

References (38)

1. K. Drlica, J. Rouviere-Yaniv, Histonelike proteins of bacteria, Microbiol. Rev. 50 (1987) 301-319.
2. G.J. Pruss, K. Drlica, DNA supercoiling and prokaryotic transcription, Cell 56 (1989) 521-523. (Pubitemid 19065526)
3. C.J. Dorman, P. Deighan, Regulation of gene expression by histone-like proteins in bacteria, Curr. Opin. Genet. Dev. 13 (2003) 179-184. (Pubitemid 36369742)
4. R.T. Dame, The role of nucleoid-associated proteins in the organization and compaction of bacterial chromatin, Mol. Microbiol. 56 (2005) 858-870.
5. J.I. Glass, N. Assad-Garcia, N. Alperovich, S. Yooseph, M.R. Lewis, M. Maruf, C.A. Hutchison 3rd, H.O. Smith, J.C. Venter, Essential genes of a minimal bacterium, Proc. Natl. Acad. Sci. U S A 103 (2006) 425-430. (Pubitemid 43122417)
6. J. Oberto, J. Rouviere-Yaniv, Serratia marcescens contains a heterodimeric HU protein like Escherichia coli and Salmonella typhimurium, J. Bacteriol. 178 (1996) 293-297. (Pubitemid 26006093)
7. J. Rouvière-Yaniv, M. Yaniv, J.E. Germond, E. coli DNA binding protein HU forms nucleosomelike structure with circular double-stranded DNA, Cell 17 (1979) 265-274. (Pubitemid 9230307)
8. A. Bensaid, A. Almeida, K. Drlica, J. Rouviere-Yaniv, Cross-talk between topoisomerase I and HU in Escherichia coli, J. Mol. Biol. 256 (1996) 292-300.
9. F. Boubrik, J. Rouviere-Yaniv, Increased sensitivity to gamma irradiation in bacteria lacking protein HU, Proc. Natl. Acad. Sci. U S A 92 (1995) 3958-3962.
10. S. Li, R. Waters, Escherichia coli strains lacking protein HU are UV sensitive due to a role for HU in homologous recombination, J. Bacteriol. 180 (1998) 3750-3756. (Pubitemid 28361566)
11. D. Bramhill, A. Kornberg, A model for initiation at origins of DNA replication, Cell 54 (1988) 915-1008.
12. K. Swinger, K. Lemberg, Y. Zhang, P. Rice, Flexible DNA bending in HU-DNA cocrystal structures, EMBO J. 22 (2003) 3749-3760. (Pubitemid 36898351)
13. K. Mouw, P. Rice, Shaping the Borrelia burgdorferi genome: crystal structure and binding properties of the DNA-bending protein Hbb, Mol. Microbiol. 63 (2007) 1319-1330.
14. J. Rouviere-Yaniv, Localization of the HU protein on the Escherichia coli nucleoid, Cold Spring Harb. Symp. Quant. Biol. 42 (1978) 439-447.
15. A. Balandina, D. Kamashev, J. Rouviere-Yaniv, The bacterial histone-like protein HU specifically recognizes similar structures in all nucleic acids. DNA, RNA, and their hybrids, J. Biol. Chem. 227 (2002) 27622-27628.
16. A. Pontiggia, A. Negri, M. Beltrame, M.E. Bianchi, Protein HU binds specifically to kinked DNA, Mol. Microbiol. 7 (1993) 343-350.
17. B. Castaing, C. Zelwer, J. Laval, S. Boiteux, HU protein of Escherichia coli binds specifically to DNA that contains single-strand breaks or gaps, J. Biol. Chem. 270 (1995) 10291-10296.
18. D. Kamashev, A. Balandina, J. Rouviere-Yaniv, The binding motif recognized by HU on both nicked and cruciform DNA, EMBO J. 18 (1999) 5434-5444. (Pubitemid 29465592)
19. D. Kamashev, J. Rouviere-Yaniv, The histone-like protein HU binds specifically to DNA recombination and repair intermediates, EMBO J. 19 (2000) 6527-6535.
20. A. Balandina, L. Claret, R. Hengge-Aronis, J. Rouviere-Yaniv, The Escherichia coli histone-like protein HU regulates rpoS translation, Mol. Microbiol. 39 (2001) 1069-1079.
21. E. Bonnefoy, J. Rouviere-Yaniv, HU and IHF, two homologous histone-like proteins of Escherichia coli, form different protein-DNA complexes with short DNA fragments, EMBO J. 10 (1991) 687-696.
22. K. Kobryn, D.Z. Naigamwalla, G. Chaconas, Site-specific DNA binding and bending by the Borrelia burgdorferi Hbb protein, Mol. Microbiol. 37 (2000) 145-155.
23. K. Swinger, P. Rice, Structure-based analysis of HU-DNA binding, J. Mol. Biol. 365 (2007) 1005-1016.
24. C. Chen, S. Ghosh, A. Grove, Substrate specificity of Helicobacter pylori histone-like HU protein is determined by insufficient stabilization of DNA flexure points, Biochem. J. 383 (2004) 343-351. (Pubitemid 39446696)
25. A. Mukherjee, G. Bhattacharyya, A. Grove, The C-terminal domain of HU-related histone-like protein Hlp from Mycobacterium smegmatis mediates DNA end-joining, Biochemistry 47 (2008) 8744-8753.
26. J. Rouviere-Yaniv, F. Gros, Characterization of a novel, low-molecular-weight DNA-binding protein from Escherichia coli, Proc. Natl. Acad. Sci. U S A 72 (1975) 3428-3432.
27. J. Oberto, E. Bonnefoy, E. Mouray, O. Pellegrini, P.M. Wikström, J. Rouvière-Yaniv, The Escherichia coli ribosomal protein S16 is an endonuclease, Mol. Microbiol. 19 (1996) 1319-1330.
28. O. Pellegrini, J. Oberto, V. Pinson, M. Wery, J. Rouviere-Yaniv, Overproduction and improved strategies to purify the threenative forms of nuclease-free HU protein, Biochimie 82 (2000) 693-704.
29. D. Kamashev, A. Balandina, A. Mazur, P. Arrimondo, J. Rouviere-Yaniv, HU binds and folds single-stranded DNA, Nucleic Acids Res. 36 (2008) 1026-1036. (Pubitemid 351267256)
30. J. Oberto, BAGET: a web server for the effortless retrieval of prokaryotic gene context and sequence, Bioinformatics 24 (2008) 424-425. (Pubitemid 351189020)
31. J. Oberto, N. Breuil, A. Hecker, F. Farina, C. Brochier-Armanet, E. Culetto, P. Forterre, Qri7/OSGEPL, the mitochondrial version of the universal Kae1/ YgjD protein, is essential for mitochondrial genome maintenance, Nucleic Acids Res. 37 (2009) 5343-5352.
32. J. Oberto, S. Nabti, V. Jooste, H. Mignot, J. Rouviere-Yaniv, The HU regulon is composed of genes responding to anaerobiosis, acid stress, high osmolarity and SOS induction, PLoS One 4 (2009) e4367.
33. F. Guo, S. Adhya, Spiral structure of Escherichia coli HUalphabeta provides foundation for DNA supercoiling, Proc. Natl. Acad. Sci. U S A 104 (2007) 4309-4314. (Pubitemid 47186222)
34. D. Esser, R. Rudolph, R. Jaenicke, G. Böhm, The HU protein from Thermotoga maritima: recombinant expression, purification and physicochemical characterization of an extremely hyperthermophilic DNA-binding protein, J. Mol. Biol. 291 (1999) 1135-1146. (Pubitemid 29423776)
35. B. Xiao, R. Johnson, J. Marko, Modulation of HU-DNA interactions by salt concentration and applied force, Nucleic Acids Res. (2010) [Epub ahead of print].
36. V. Pinson, M. Takahashi, J. Rouviere-Yaniv, Differential binding of the Escherichia coli HU, homodimeric forms and heterodimeric form to linear, gapped and cruciform DNA, J. Mol. Biol. 287 (1999) 485-497. (Pubitemid 29168428)
37. O. Huisman, M. Faelen, D. Girard, A. Jaffe, A. Toussaint, J. Rouviere-Yaniv, Multiple defects in Escherichia coli mutants lacking HU protein, J. Bacteriol. 171 (1989) 3704-3712. (Pubitemid 19174141)
38. N. Groch, H. Schindelin, A.S. Scholtz, U. Hahn, U. Heinemann, Determination of DNA-binding parameters for the Bacillus subtilis histone-like HBsu protein through introduction of fluorophores by site-directed mutagenesis of a synthetic gene, Eur. J. Biochem. 207 (1992) 677-685.