Catalytic and chaperone-like functions in an intrinsically disordered protein associated with desiccation tolerance

Proceedings of the National Academy of Sciences of the United States of America

Volumn 107, Issue 37, 2010, Pages 16084-16089

  Chakrabortee, Sohini ^a   Meersman, Filip ^b   Kaminski Schierle, Gabriele S ^a   Bertoncini, Carlos W ^a,d   McGee, Brian ^a   Kaminski, Clemens F ^a,c   Tunnacliffe, Alan ^a  

^a UNIVERSITY OF CAMBRIDGE   (United Kingdom)

^b UNIVERSITY OF LEUVEN   (Belgium)

^c MAX PLANCK INSTITUTE FOR THE SCIENCE OF LIGHT   (Germany)

^d INSTITUTE FOR RESEARCH IN BIOMEDICINE   (Spain)

Author keywords

Anhydrobiosis; Endonuclease; Intrinsically unstructured protein; Molecular shield; Natively unfolded protein

Indexed keywords

ALANINE; ANHYDRIN; CHAPERONE; ENDONUCLEASE; INTRINSICALLY DISORDERED PROTEIN; MEMBRANE PROTEIN; UNCLASSIFIED DRUG; DNA; PROTEIN BINDING;

ANHYDROBIOSIS; ARTICLE; CATALYSIS; CHROMATIN; CONTROLLED STUDY; DESSICATION TOLERANCE; DNA DAMAGE; DNA SUPERCOILING; ENZYME ACTIVE SITE; ENZYME ACTIVITY; HUMAN CELL CULTURE; IN VITRO STUDY; IN VIVO STUDY; NUCLEUS ACCUMBENS; OCULOPHARYNGEAL MUSCULAR DYSTROPHY; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; AMINO ACID SEQUENCE; ANIMAL; BIOCATALYSIS; CELL LINE; CHEMISTRY; DESICCATION; HUMAN; METABOLISM; MOLECULAR GENETICS; TYLENCHIDA;

APHELENCHUS AVENAE; EUKARYOTA;

AMINO ACID SEQUENCE; ANIMALS; BIOCATALYSIS; CELL LINE; DESICCATION; DNA; HUMANS; MOLECULAR CHAPERONES; MOLECULAR SEQUENCE DATA; PROTEIN BINDING; TYLENCHIDA;

EID: 77958011138     PISSN: 00278424     EISSN: 10916490     Source Type: Journal    
DOI: 10.1073/pnas.1006276107     Document Type: Article

References (36)

1. Tunnacliffe A, Wise MJ (2007) The continuing conundrum of the LEA proteins. Naturwissenschaften 94:791-812.
2. Tompa P (2009) Structure and Function of Intrinsically Disordered Proteins (Taylor and Francis, Boca Raton, FL).
3. Oldfield CJ, et al. (2005) Comparing and combining predictors of mostly disordered proteins. Biochemistry 44:1989-2000.
4. Pentony MM, Jones DT (2010) Modularity of intrinsic disorder in the human proteome. Proteins 78:212-221.
5. Ward JJ, Sodhi JS, McGuffin LJ, Buxton BF, Jones DT (2004) Prediction and functional analysis of native disorder in proteins from the three kingdoms of life. J Mol Biol 337:635-645.
6. Dunker AK, Obradovic Z, Romero P, Garner EC, Brown CJ (2000) Intrinsic protein disorder in complete genomes. Genome Inform Ser Workshop Genome Inform 11:161-171.
7. Dunker AK, et al. (2001) Intrinsically disordered protein. J Mol Graph Model 19:26-59.
8. Dyson HJ,Wright PE (2002) Coupling of folding and binding for unstructured proteins. Curr Opin Struc Biol 12:54-60.
9. Wright PE, Dyson HJ (2009) Linking folding and binding. Curr Opin Struc Biol 19:31-38.
10. Russo AA, Jeffrey PD, Patten AK, Massague J, Pavletich NP (1996) Crystal structure of the p27(Kip1) cyclin-dependent-kinase inhibitor bound to the cyclin A Cdk2 complex. Nature 382:325-331. (Pubitemid 26260452)
11. Lacy ER, et al. (2004) p27 binds cyclin-CDK complexes through a sequential mechanism involving binding-induced protein folding. Nat Struct Mol Biol 11:358-364.
12. Tompa P, Fuxreiter M (2008) Fuzzy complexes: Polymorphism and structural disorder in protein-protein interactions. Trends Biochem Sci 33:2-8.
13. Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27:527-533.
14. Mukhopadhyay R, Kumar S, Hoh JH (2004) Molecular mechanisms for organizing the neuronal cytoskeleton. Bioessays 26:1017-1025.
15. Chakrabortee S, et al. (2007) Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function. Proc Natl Acad Sci USA 104:18073-18078. (Pubitemid 350210822)
16. Goyal K, et al. (2003) Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J Biol Chem 278:12977-12984. (Pubitemid 36800064)
17. Kovacs D, Kalmar E, Torok Z, Tompa P (2008) Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins. Plant Physiol 147:381-390. (Pubitemid 352844363)
18. Browne JA, et al. (2004) Dehydration-specific induction of hydrophilic protein genes in the anhydrobiotic nematode Aphelenchus avenae. Eukaryot Cell 3:966-975.
19. Goyal K, Walton LJ, Tunnacliffe A (2005) LEA proteins prevent protein aggregation due to water stress. Biochem J 388:151-157.
20. Lee BJ, et al. (2006) Rules for nuclear localization sequence recognition by karyopherin beta 2. Cell 126:543-558.
21. Davies JE, Sarkar S, Rubinsztein DC (2006) Trehalose reduces aggregate formation and delays pathology in a transgenic mouse model of oculopharyngeal muscular dystrophy. Hum Mol Genet 15:23-31.
22. Davies JE, Berger Z, Rubinsztein DC (2006) Oculopharyngeal muscular dystrophy: Potential therapies for an aggregate-associated disorder. Int J Biochem Cell Biol 38:1457-1462.
23. Saibil HR (2008) Chaperone machines in action. Curr Opin Struc Biol 18:35-42.
24. Tam S, et al. (2009) The chaperonin TRiC blocks a huntingtin sequence element that promotes the conformational switch to aggregation. Nat Struct Mol Biol 16:1279-1285.
25. Davies JE, Sarkar S, Rubinsztein DC (2008) Wild-type PABPN1 is anti-apoptotic and reduces toxicity of the oculopharyngeal muscular dystrophy mutation. Hum Mol Genet 17:1097-1108. (Pubitemid 351505885)
26. Elder AD, et al. (2009) A quantitative protocol for dynamic measurements of protein interactions by Forster resonance energy transfer-sensitized fluorescence emission. J R Soc Interface 6:S59-S81.
27. Jeffery CJ (2009) Moonlighting proteins - An update. Mol Biosyst 5:345-350.
28. Tompa P, Szasz C, Buday L (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30:484-489. (Pubitemid 41206503)
29. Oldfield CJ, et al. (2008) Flexible nets: Disorder and induced fit in the associations of p53 and 14-3-3 with their partners. BMC Genomics 9(Suppl 1):S1.
30. Bright JN, Woolf TB, Hoh JH (2001) Predicting properties of intrinsically unstructured proteins. Prog Biophys Mol Biol 76:131-173.
31. Napper DH (1983) Polymeric stabilization of colloidal dispersions (Academic, London).
32. Zhou EH, et al. (2009) Universal behavior of the osmotically compressed cell and its analogy to the colloidal glass transition. Proc Natl Acad Sci USA 106:10632-10637.
33. Choe KP, Strange K (2008) Genome-wide RNAi screen and in vivo protein aggregation reporters identify degradation of damaged proteins as an essential hypertonic stress response. Am J Physiol-Cell Ph 295:C1488-1498.
34. Uversky V, Gillespie J, Fink A (2000) Why are "natively unfolded" proteins unstructured under physiologic conditions? Proteins 41:415-427.
35. Cho HS, et al. (1996) Yeast heat shock transcription factor N-terminal activation domains are unstructured as probed by heteronuclear NMR spectroscopy. Protein Sci 5:262-269.
36. Sigalov AB, Zhuravleva AV, Orekhov VY (2007) Binding of intrinsically disordered proteins is not necessarily accompanied by a structural transition to a folded form. Biochimie 89:419-421.