Structural and aggregation behavior of the human γD-crystallin mutant E107A, associated with congenital nuclear cataract

Molecular Vision

Volumn 16, Issue , 2010, Pages 2822-2828

  Vendra, Venkata Pulla Rao ^a   Balasubramanian, Dorairajan ^a  

^a L V PRASAD EYE INSTITUTE   (India)

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENTARY DNA; FLUORESCENT DYE; GAMMA CRYSTALLIN; GAMMA D CRYSTALLIN; GUANIDINE; MUTANT PROTEIN; NILE RED; UNCLASSIFIED DRUG;

ARTICLE; CATARACTOGENESIS; CIRCULAR DICHROISM; CONGENITAL CATARACT; CONTROLLED STUDY; DISEASE ASSOCIATION; FLUORESCENCE SPECTROSCOPY; GENETIC TRANSFECTION; HELA CELL; HUMAN; HUMAN CELL; HUMAN TISSUE; IMMUNOFLUORESCENCE TEST; IN VITRO STUDY; LENS; LENS EPITHELIUM; LIGHT SCATTERING; MOLECULAR CLONING; POINT MUTATION; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CONFORMATION; PROTEIN DENATURATION; PROTEIN EXPRESSION; PROTEIN ISOLATION; PROTEIN PURIFICATION; PROTEIN SECONDARY STRUCTURE; PROTEIN STABILITY; PROTEIN STRUCTURE; PROTEIN TERTIARY STRUCTURE; SOLUBILITY; WILD TYPE;

CATARACT; CELL LINE; GAMMA-CRYSTALLINS; HUMANS; LENS NUCLEUS, CRYSTALLINE; MICROSCOPY, CONFOCAL; MUTANT PROTEINS; MUTATION; PROTEIN STRUCTURE, QUATERNARY; TRANSFECTION;

EID: 78650800045     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

References (22)

1. Vanita V, Singh JR, Singh D, Varon R, Sperling K. Novel mutation in the γ-S crystallin gene causing autosomal dominant cataract. Mol Vis 2009; 15:476-81. [PMID: 19262743]
2. Roshan M, Vijaya PH, Lavanya GR, Shama PK, Santhiya ST, Graw J, Gopinath PM, Satyamoorthy K. A novel human CRYD mutation in juvenile autosomal dominant cataract. Mol Vis 2010; 16:887-96. [PMID: 20508808]
3. Das P, King JA, Zhou R. β-Strand interactions at the domain interface critical for the stability of human lens γD-crystallin. Protein Sci 2010; 19:131-40. [PMID: 19937657]
4. Kosinski-Collins MS, King J. In vitro unfolding, refolding, and polymerization of human gamma D crystallin, a protein involved in cataract formation. Protein Sci 2003; 12:480-90. [PMID: 12592018]
5. Pande A, Ghosh KS, Banerjee PR, Pande J. Increase in surface hydrophobicity of the cataract-associated P23T mutant of human γD-crystallin is responsible for its dramatically lower, retrograde solubility. Biochemistry 2010; 49:6122-9. [PMID: 20553008]
6. Pande A, Zhang J, Banerjee PR, Puttamadappa SS, Shekhtman A, Pande J. NMR study of the cataract-linked P23T mutant of human gamma D-crystallin shows minor changes in hydrophobic patches that reflect its retrograde solubility. Biochem Biophys Res Commun 2009; 382:196-9. [PMID: 19275895]
7. McManus JJ, Lomakin A, Ogun O, Pande A, Basam M, Pande J, Benedek JB. Altered phase diagram due to a single point mutation in human γD-crystallin. Proc Natl Acad Sci USA 2007; 104:16856-61. [PMID: 17923670]
8. Messina-Baas OM, Gonzalez-Huerta LM, Cuevas-Covarrubias SA. Two affected siblings with nuclear cataract associated with a novel missense mutation in the CRYGD gene. Mol Vis 2006; 12:995-1000. [PMID: 16943771]
9. Mills IA, Flaugh SL, Kosinski-Collins MS, King JA. Folding and stability of the isolated Greek key domains of the longlived human lens proteins γD-crystallin and γS-crystallin. Protein Sci 2007; 16:2427-44. [PMID: 17905830]
10. Mandal K, Kono M, Bose SK, Thomson J, Chakrabarti B. Structure and stability of gamma-crystallins, IV: aggregation and structural destabilization in photosensitized reactions. Photochem Photobiol 1988; 47:583-91. [PMID: 3406121]
11. Sutter M, Oliviera S, Sanders NN, Lucas B, van Hoek A, Hink MA, Visser AJ, De Smedt SC, Hennink WE, Jiskoot W. Sensitive spectroscopic detection of large and denatured protein aggregates in solution by use of the fluorescent dye Nile Red. J Fluoresc 2007; 17:181-92. [PMID: 17294134]
12. Demeule B, Gurny R, Arvinte T. Detection and characterization of protein aggregates by fluorescence microscopy. Int J Pharm 2007; 329:37-45. [PMID: 17005340]
13. www.rsbweb.nih.gov/ij
14. Liu B-F, Song S, Hanson M, Liang JJ-N. Protein-protein interactions involving congenital cataract T5P γC-crystallin mutant: a confocal fluorescence microscopy study. Exp Eye Res 2008; 87:515-20. [PMID: 18926820]
15. Talla V, Srinivasan N, Balasubramanian D. Visualization of in situ intracellular aggregation of two cataract-associated human γ-crystallin mutants: lose a tail, lose transparency. Invest Ophthalmol Vis Sci 2008; 49:3483-90. [PMID: 18421082]
16. Wang K, Cheng C, Li L, Liu H, Huang Q, Xia CH, Yao K, Sun P, Horwitz J, Gong X. γD-Crystallin-associated protein aggregation and lens fiber cell denucleation. Invest Ophthalmol Vis Sci 2007; 48:3719-28. [PMID: 17652744]
17. Pigaga V, Quinlan RA. Lenticular chaperones suppress the aggregation of the cataract-causing mutant T5P γC-crystallin. Exp Cell Res 2006; 312:51-62. [PMID: 16303126]
18. ExPASy (Expert Protein Analysis System) proteomics server- ProtParam tool. www.expasy.ch/tools/protparam.html.
19. Pande A, Annunziata O, Asherie N, Ogun O, Benedek GB, Pande J. Decrease in protein solubility and cataract formation caused by the Pro23 to Thr mutation in human gamma Dcrystallin. Biochemistry 2005; 44:2491-500. [PMID: 15709761]
20. Jung J, Byeon IJ, Wang Y, King J, Gronenborn AM. The structure of the cataract-causing P23T mutant of human gamma D-crystallin exhibits distinctive local conformational and dynamic changes. Biochemistry 2009; 48:2597-609. [PMID: 19216553]
21. Carson M, Johnson DH, McDonald H, Brouillette C, DeLucas LJ. His-tag impact on structure. Acta Crystallogr D Biol Crystallogr 2007; 63:295-301. [PMID: 17327666]
22. Stevens JC, Chia R, Hendriks WT, Bros-Faser V, van Minnen J, Martin JE, Jackson GS, Greensmith L, Schiavo G, Fisher EM. Modification of superoxide dismutase 1 (SOD1) properties by a GFP tag- implications for research into amyotropic lateral sclerosis (ALS). PLoS ONE 2010; 5:e9541. [PMID: 20221404]