Correction: Reduced stability and increased dynamics in the human Proliferating Cell Nuclear Antigen (PCNA) relative to the yeast homolog (PLoS ONE (2011) 6, 2 (e16600) DOI:10.1371/journal.pone.0016600);Reduced stability and increased dynamics in the human Proliferating Cell Nuclear Antigen (PCNA) relative to the yeast homolog

PLoS ONE

Volumn 6, Issue 2, 2011, Pages

  de Biasio, Alfredo ^a   Sánchez, Ricardo ^a   Prieto, Jesús ^b   Villate, Maider ^a   Campos Olivas, Ramón ^b   Blanco, Francisco J ^a,c  

^a CIC BIOGUNE   (Spain)

^b Centro Nacional de Investigaciones Oncológicas   (Spain)

^c BASQUE FOUNDATION FOR SCIENCE   (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

AMIDE; CYCLINE; FUNGAL PROTEIN; CELL NUCLEUS ANTIGEN; POL30 PROTEIN, S CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEIN;

ALPHA HELIX; ARTICLE; BETA SHEET; BINDING AFFINITY; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; CRYSTAL STRUCTURE; FUNCTIONAL MORPHOLOGY; HUMAN; HUMAN VERSUS NONHUMAN DATA; MOLECULAR DYNAMICS; MOLECULAR EVOLUTION; NONHUMAN; PROTEIN DENATURATION; PROTEIN DNA INTERACTION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN STABILITY; SEQUENCE HOMOLOGY; SIGNAL TRANSDUCTION; STRUCTURAL HOMOLOGY; THERMODYNAMICS; TRANSIENT EXPRESSION; AMINO ACID SEQUENCE; CHEMICAL STRUCTURE; CHEMISTRY; COMPARATIVE STUDY; DOWN REGULATION; METABOLISM; MOLECULAR GENETICS; PHYSIOLOGY; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; SACCHAROMYCES CEREVISIAE; SPECIES DIFFERENCE; UPREGULATION; YEAST;

RUMEX; SACCHAROMYCETALES;

AMINO ACID SEQUENCE; ANTIGENS, NUCLEAR; DOWN-REGULATION; HUMANS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PROLIFERATING CELL NUCLEAR ANTIGEN; PROTEIN BINDING; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN STABILITY; PROTEIN STRUCTURE, SECONDARY; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; SEQUENCE HOMOLOGY; SPECIES SPECIFICITY; THERMODYNAMICS; UP-REGULATION; YEASTS;

EID: 79951996226     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0097057     Document Type: Erratum

References (44)

1. Pomerantz RT, O'Donnell M, (2007) Replisome mechanics: insights into a twin DNA polymerase machine. Trends Microbiol 15: 156-164.
2. Moldovan GL, Pfander B, Jentsch S, (2007) PCNA, the maestro of the replication fork. Cell 129: 665-679.
3. Kong XP, Onrust R, O'Donnell M, Kuriyan J, (1992) Three-dimensional structure of the beta subunit of E. coli DNA polymerase III holoenzyme: a sliding DNA clamp. Cell 69: 425-437.
4. Krishna TS, Kong XP, Gary S, Burgers PM, Kuriyan J, (1994) Crystal structure of the eukaryotic DNA polymerase processivity factor PCNA. Cell 79: 1233-1243.
5. Matsumiya S, Ishino Y, Morikawa K, (2001) Crystal structure of an archaeal DNA sliding clamp: proliferating cell nuclear antigen from Pyrococcus furiosus. Protein Sci 10: 17-23.
6. Schurtenberger P, Egelhaaf SU, Hindges R, Maga G, Jonsson ZO, et al. (1998) The solution structure of functionally active human proliferating cell nuclear antigen determined by small-angle neutron scattering. J Mol Biol 275: 123-132.
7. Burgers PM, Yoder BL, (1993) ATP-independent loading of the proliferating cell nuclear antigen requires DNA ends. J Biol Chem 268: 19923-19926.
8. Tsurimoto T, Stillman B, (1991) Replication factors required for SV40 DNA replication in vitro. I. DNA structure-specific recognition of a primer-template junction by eukaryotic DNA polymerases and their accessory proteins. J Biol Chem 266: 1950-1960.
9. Warbrick E, (2000) The puzzle of PCNA's many partners. Bioessays 22: 997-1006.
10. Maga G, Hubscher U, (2003) Proliferating cell nuclear antigen (PCNA): a dancer with many partners. J Cell Sci 116: 3051-3060.
11. Campos-Olivas R, Sanchez R, Torres D, Blanco FJ, (2007) Backbone assignment of the 98 kDa homotrimeric yeast PCNA ring. J Biomol NMR 38: 167.
12. Sanchez R, Torres D, Prieto J, Blanco FJ, Campos-Olivas R, (2007) Backbone assignment of human proliferating cell nuclear antigen. Biomol NMR Assign 1: 245-247.
13. Deckert G, Warren PV, Gaasterland T, Young WG, Lenox AL, et al. (1998) The complete genome of the hyperthermophilic bacterium Aquifex aeolicus. Nature 392: 353-358.
14. Yao N, Turner J, Kelman Z, Stukenberg PT, Dean F, et al. (1996) Clamp loading, unloading and intrinsic stability of the PCNA, beta and gp45 sliding clamps of human, E. coli and T4 replicases. Genes Cells 1: 101-113.
15. Naryzhny SN, Zhao H, Lee H, (2005) Proliferating cell nuclear antigen (PCNA) may function as a double homotrimer complex in the mammalian cell. J Biol Chem 280: 13888-13894.
16. Bowie JU, Sauer RT, (1989) Equilibrium dissociation and unfolding of the Arc repressor dimer. Biochemistry 28: 7139-7143.
17. Karshikoff A, Ladenstein R, (2001) Ion pairs and the thermotolerance of proteins from hyperthermophiles: a traffic rule for hot roads. Trends Biochem Sci 26: 550-556.
18. Bohm G, Jaenicke R, (1994) Relevance of sequence statistics for the properties of extremophilic proteins. Int J Pept Protein Res 43: 97-106.
19. Choe SE, Matsudaira PT, Osterhout J, Wagner G, Shakhnovich EI, (1998) Folding kinetics of villin 14T, a protein domain with a central beta-sheet and two hydrophobic cores. Biochemistry 37: 14508-14518.
20. Guthe S, Kapinos L, Moglich A, Meier S, Grzesiek S, et al. (2004) Very fast folding and association of a trimerization domain from bacteriophage T4 fibritin. J Mol Biol 337: 905-915.
21. Guidry JJ, Moczygemba CK, Steede NK, Landry SJ, Wittung-Stafshede P, (2000) Reversible denaturation of oligomeric human chaperonin 10: denatured state depends on chemical denaturant. Protein Sci 9: 2109-2117.
22. Hlinkova V, Xing G, Bauer J, Shin YJ, Dionne I, et al. (2008) Structures of monomeric, dimeric and trimeric PCNA: PCNA-ring assembly and opening. Acta Crystallogr D Biol Crystallogr 64: 941-949.
23. Dempsey, (2001) Hydrogen Exchange in Peptides and Proteins Using NMR spectroscopy. Prog Nucl Magn Reson Spectrosc 39: 135-170.
24. Hernandez G, Jenney FE Jr, Adams MW, LeMaster DM, (2000) Millisecond time scale conformational flexibility in a hyperthermophile protein at ambient temperature. Proc Natl Acad Sci U S A 97: 3166-3170.
25. Ishima R, Torchia DA, (2000) Protein dynamics from NMR. Nat Struct Biol 7: 740-743.
26. Pantoja-Uceda D, Arolas JL, Garcia P, Lopez-Hernandez E, Padro D, et al. (2008) The NMR structure and dynamics of the two-domain tick carboxypeptidase inhibitor reveal flexibility in its free form and stiffness upon binding to human carboxypeptidase B. Biochemistry 47: 7066-7078.
27. Georgescu RE, Kim SS, Yurieva O, Kuriyan J, Kong XP, et al. (2008) Structure of a sliding clamp on DNA. Cell 132: 43-54.
28. Tokuriki N, Tawfik DS, (2009) Stability effects of mutations and protein evolvability. Curr Opin Struct Biol 19: 596-604.
29. Uversky VN, (2002) What does it mean to be natively unfolded? Eur J Biochem 269: 2-12.
30. Tompa P, Szasz C, Buday L, (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30: 484-489.
31. Pascal JM, Tsodikov OV, Hura GL, Song W, Cotner EA, et al. (2006) A flexible interface between DNA ligase and PCNA supports conformational switching and efficient ligation of DNA. Mol Cell 24: 279-291.
32. Kontopidis G, Wu SY, Zheleva DI, Taylor P, McInnes C, et al. (2005) Structural and biochemical studies of human proliferating cell nuclear antigen complexes provide a rationale for cyclin association and inhibitor design. Proc Natl Acad Sci U S A 102: 1871-1876.
33. Chapados BR, Hosfield DJ, Han S, Qiu J, Yelent B, et al. (2004) Structural basis for FEN-1 substrate specificity and PCNA-mediated activation in DNA replication and repair. Cell 116: 39-50.
34. Sakurai S, Kitano K, Yamaguchi H, Hamada K, Okada K, et al. (2005) Structural basis for recruitment of human flap endonuclease 1 to PCNA. EMBO J 24: 683-693.
35. Shell SS, Putnam CD, Kolodner RD, (2007) The N terminus of Saccharomyces cerevisiae Msh6 is an unstructured tether to PCNA. Mol Cell 26: 565-578.
36. Fridman Y, Palgi N, Dovrat D, Ben-Aroya S, Hieter P, et al. Subtle alterations in PCNA-partner interactions severely impair DNA replication and repair. PLoS Biol 8: e1000507.
37. Pace CN, (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves. Methods Enzymol 131: 266-280.
38. Greene RF Jr, Pace CN, (1974) Urea and guanidine hydrochloride denaturation of ribonuclease, lysozyme, alpha-chymotrypsin, and beta-lactoglobulin. J Biol Chem 249: 5388-5393.
39. Venters RA, Farmer BT 2nd, Fierke CA, Spicer LD, (1996) Characterizing the use of perdeuteration in NMR studies of large proteins: 13C, 15N and 1H assignments of human carbonic anhydrase II. J Mol Biol 264: 1101-1116.
40. Pervushin KV, WGKW (1998) Single transition-to-single transition polarization transfer (ST2-PT) in [15N,1H]-TROSY. J Biomol NMR 12: 345-348.
41. Fogh R, Ionides J, Ulrich E, Boucher W, Vranken W, et al. (2002) The CCPN project: an interim report on a data model for the NMR community. Nat Struct Biol 9: 416-418.
42. Zhang YZ, (2007) Protein and peptide structure and interactions studied by hydrogen exchange and NMR, PhD Thesis Philadelphia: University of Pennsylvania, PA.
43. Kontopidis G, McInnes C, Pandalaneni SR, McNae I, Gibson D, et al. (2006) Differential binding of inhibitors to active and inactive CDK2 provides insights for drug design. Chem Biol 13: 201-211.
44. Wishart DS, Sykes BD, (1994) The 13C chemical-shift index: a simple method for the identification of protein secondary structure using 13C chemical-shift data. J Biomol NMR 4: 171-180.