Folding is coupled to dimerization of Tctex-1 dynein light chain

Biochemistry

Volumn 45, Issue 22, 2006, Pages 6793-6800

  Talbott, Matthew ^b   Hare, Michael ^a   Nyarko, Afua ^a   Hays, Thomas S ^c   Barbar, Elisar ^a  

^a OREGON STATE UNIVERSITY   (United States)

^b OHIO UNIVERSITY   (United States)

^c UNIVERSITY OF MINNESOTA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ANISOTROPY; CROSSLINKING; DIMERIZATION; FLUORESCENCE; MONOMERS; SEDIMENTATION;

DENATURANTS; PREMELTING CONFORMATIONAL DISORDER; SEDIMENTATION EQUILIBRIUM; UNFOLDING TRANSITION;

DIMERS;

DYNEIN ADENOSINE TRIPHOSPHATASE; TCTEX 1 PROTEIN; UNCLASSIFIED DRUG;

ANISOTROPY; ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; CROSS LINKING; DIMERIZATION; FLUORESCENCE; LIGHT CHAIN; PRIORITY JOURNAL; PROTEIN FOLDING; SEDIMENTATION; THERMOSTABILITY;

ANIMALS; DIMERIZATION; DISSOCIATIVE DISORDERS; DROSOPHILA PROTEINS; DYNEIN ATPASE; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 33744953791     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi0600345     Document Type: Article

References (51)

1. Allan, V. J., Thompson, H. M., and McNiven, M. A. (2002) Motoring around the Golgi, Nat. Cell Biol. 4, E236-E242.
2. Harada, A., and Hirokawa, N. (1999) The role of cytoplasmic dynein in the ER to Golgi transport, Mol. Biol. Cell 10, 2126.
3. Li, M., McGrail, M., Serr, M., and Hays, T. S. (1994) Drosophila cytoplasmic dynein, a microtubule motor that is asymmetrically localized in the oocyte, J. Cell Biol. 126, 1475-1494.
4. McGrail, M., and Hays, T. S. (1997) The microtubule motor cytoplasmic dynein is required for spindle orientation during germline cell divisions and oocyte differentiation in Drosophila, Development 124, 2409-2419.
5. Vallee, R. B., Williams, J. C., Varma, D., and Barnhart, L. E. (2004) Dynein: An ancient motor protein involved in multiple modes of transport, J. Neurobiol. 58, 189-200.
6. Vale, R. D. (2003) The molecular motor toolbox for intracellular transport, Cell 112, 467-480.
7. Susalka, S. J., and Pfister, K. K. (2000) Cytoplasmic dynein subunit heterogeneity: Implications for axonal transport, J. Neurocytol. 29, 819-829.
8. Tai, A. W., Chuang, J. Z., and Sung, C. H. (2001) Cytoplasmic dynein regulation by subunit heterogeneity and its role in apical transport, J. Cell Biol. 153, 1499-1509.
9. Bowman, A. B., Patel-King, R. S., Benashski, S. E., McCaffery, J. M., Goldstein, L. S. B., and King, S. M. (1999) Drosophila roadblock and Chlamydomonas LC7: A conserved family of dynein-associated proteins involved in axonalteansport, flagellar motility, and mitosis, J. Cell Biol. 146, 165-179.
10. Li, M. G., Serr, M., Newman, E. A., and Hays, T. S. (2004) The Drosophila tctex-1 light chain is dispensable for essential cytoplasmic dynein functions but is required during spermatid differentiation, Mol. Biol. Cell 15, 3005-2014.
11. Tai, A. W., Chuang, J. Z., Bode, C., Wolfram, U., and Sung, C. H. (1999) Rhodopsin's carboxy-terminal cytoplasmic tail acts as a membrane receptor for cytoplasmic dynein by binding to the dynein light chain Tctex-1, Cell 97, 877-887.
12. Tai, A. W., Chuang, J. Z., and Sung, C. H. (1998) Localization of Tctex-1, a cytoplasmic dynein light chain, to the golgi apparatus and evidence for dynein complex heterogeneity, J. Biol. Chem. 273, 19639-19649.
13. Makokha, M., Hare, M., Li, M., Hays, T., and Barbar, E. (2002) Interactions of cytoplasmic dynein light chains Tctex-1 and LC8 with the intermediate chain IC74, Biochemistry 41, 4302-4311.
14. Mok, Y. K., Lo, K. W. H., and Zhang, M. J. (2001) Structure of Tctex-1 and its interaction with cytoplasmic dynein intermediate chain, J. Biol. Chem. 276, 14067-14074.
15. King, S. M., Barbarese, E., Dillman, J. F., Benashski, S. E., Do, K. T., Patel-King, R. S., and Pfister, K. K (1998) cytoplasmic dynein contains a family of differentially expressed light chains, Biochemistry 37, 15033-15041.
16. Campbell, K. S., Cooper, S., Dessing, M., Yates, S., and Buder, A. (1998) Interaction of p59(fyn) kinase with the dynein light chain, Tctex-1, and colocalization during cytokinesis, J. Immunol. 161, 1728-1737.
17. Yano, H., Lee, F. S., Kong, H., Chuang, J. Z., Arevalo, J. C., Perez, P., Sung, C. H., and Chao, M. V. (2001) Association of Trk neurotrophin receptors with components of the cytoplasmic dynein motor, J. Neurosci. 21, U7-U13.
18. Chuang, J. Z., Yeh, T. Y., Bollati, F., Conde, C., Canavosio, F., Caceres, A., and Sung, C. H. (2005) The dynein light chain Tctex-1 has a dynein-independent role in actin remodeling during neurite outgrowth, Dev. Cell 9, 75-86.
19. Makokha, M., and Barbar, E. (2001) Physical characterization of Tctex-1, a dynein light chain: Dimerization, folding and role in dynein assembly, Biophys. J. 80, 2530.
20. DiBella, L. M., Benashski, S. E., Tedford, H. W., Karrison, A., Patel-King, R. S., and King, S. M. (2001) The Tctex1/Tctex2 class of dynein light chains-Dimerization, differential expression, and interaction with the LC8 protein family, J. Biol. Chem. 276, 14366-14373.
21. Williams, J. C., Xie, H., and Hendrickson, W. A. (2005) Crystal structure of dynein light chain TCTEX-1, J. Biol. Chem. 280, 21981-21986.
22. Wu, H., Maciejewski, M. W., Takebe, S., and King, S. M. (2005) Solution structure of the Tctex1 dimer reveals a mechanism for dynein-cargo interactions, Structure (London) 13, 213-223.
23. Liang, J., Jaffrey, S. R., Guo, W., Snyder, S. H., and Clardy, J. (1999) Structure of the PIN/LC8 dimer with a bound peptide, Nat. Struct. Biol. 6, 735-740.
24. Mei, G., Di Venere, A., Rosato, N., and Finazzi-Agro, A. (2005) The importance of being dimeric, FEBS J. 272, 16-27.
25. Steif, C., Weber, P., Hinz, H. J., Flossdorf, J., Cesareni, G., and Kokkinidis, M. (1993) Subunit interactions provide a significant contribution to the stability of the dimeric four-alpha-helical-bundle protein ROP, Biochemistry 32, 3867-3876.
26. Bowie, J. U., and Sauer, R. T. (1989) Equilibrium dissociation and unfolding of the Arc repressor dimer, Biochemistry 28, 7139-7143.
27. Gittelman, M. S., and Matthews, C. R. (1990) Folding and stability of trp aporepressor from Escherichia coli, Biochemistry 29, 7011-7020.
28. Grant, S. K., Deckman, I. C., Culp, J. S., Minnich, M. D., Brooks, I. S., Hensley, P., Debouck, C., and Meek, T. D. (1992) Use of protein unfolding studies to determine the conformational and dimeric stabilities of HIV-1 and SIV proteases, Biochemistry 31, 9491-9501.
29. Topping, T. B., Hoch, D. A., and Gloss, L. M. (2004) Folding mechanism of FIS, the intertwined, dimeric factor for inversion stimulation, J. Mol. Biol. 335, 1065-1081.
30. Barbar, E., Kleinman, B., Imhoff, D., Li, M. G., Hays, T. S., and Hare, M. (2001) Dimerization and folding of LC8, a highly conserved light chain of cytoplasmic dynein, Biochemistry 40, 1596-1605.
31. Nyarko, A., Cochrun, L., Norwood, S., Pursifull, N., Voth, A., and Barbar, E. (2005) Ionization of His 55 at the dimer interface of dynein light-chain LC8 is coupled to dimer dissociation, Biochemistry 44, 14248-14255.
32. Wang, L., Hare, M., Hays, T. S., and Barbar, E. (2004) Dynein light chain LC8 promotes assembly of the coiled-coil domain of swallow protein, Biochemistry 43, 4611-4620.
33. Pace, C. N., and Scholtz, J. M. (1997) in Protein Structure: A Practical Approach (Creighton, T. E., Ed.) pp 299-322, Oxford University Press, Oxford, U.K.
34. Pace, C. N. (1986) Determination and analysis of urea and guanidine hydrochloride denaturation curves, Methods Enzymol. 131, 266-280.
35. Neet, K. E., and Timm, D. E. (1994) Conformational stability of dimeric proteins: Quantitative studies by equilibrium denaturation, Protein Sci. 3, 2167-2174.
36. Ramsay, G. D., and Eftink, M. R. (1994) Analysis of multidimensional spectroscopic data to monitor unfolding of proteins, Methods Enzymol. 240, 615-645.
37. Runnels, L. W., and Scarlata, S. F. (1995) Theory and application of fluorescence homotransfer to melittin oligomerization, Biophys. J. 69, 1569-1583.
38. Imoto, T., Forster, L. S., Rupley, J. A., and Tanaka, F. (1972) Fluorescence of lysozyme: Emissions from tryptophan residues 62 and 108 and energy migration, Proc. Natl. Acad. Sci. U.S.A. 69, 1151-1155.
39. Richards, F. M., and Knowles, J. R. (1968) Glutaraldehyde as a protein cross-linkage reagent, J. Mol. Biol. 37, 231-233.
40. Timm, D. E., and Neet, K. E. (1992) Equilibrium denaturation studies of mouse beta-nerve growth-factor, Protein Sci. 1, 236-244.
41. Myers, J. K., Pace, C. N., and Scholtz, J. M. (1995) Denaturant m values and heat capacity changes: Relation to changes in accessible surface areas of protein unfolding, Protein Sci. 4, 2138-2148.
42. Karplus, M., and Petsko, G. A. (1990) Molecular dynamics simulations in biology, Nature 347, 631-639.
43. Eftink, M. R. (1994) The use of fluorescence methods to monitor unfolding transitions in proteins, Biophys. J. 66, 482-501.
44. Chen, Y., and Barkley, M. D. (1998) Toward understanding tryptophan fluorescence in proteins, Biochemistry 37, 9976-9982.
45. Makokha, M., Huang, Y. J., Montelione, G., Edison, A. S., and Barbar, E. (2004) The solution structure of the pH-induced monomer of dynein light-chain LC8 from Drosophila, Protein Sci. 13, 727-734.
46. Mann, C. J., Royer, C. A., and Matthews, C. R. (1993) Tryptophan replacements in the trp aporepressor from Escherichia coli: Probing the equilibrium and kinetic folding models, Protein Sci. 2, 1853-1861.
47. Aim, E., and Baker, D. (1999) Matching theory and experiment in protein folding, Curr. Opin. Struct. Biol 9, 189-196.
48. Wallace, L. A., and Matthews, C. R. (2002) Sequential vs. parallel protein-folding mechanisms: Experimental tests for complex folding reactions, Biophys. Chem. 101-102, 113-131.
49. Vallee-Belisle, A., Turcotte, J. F., and Michnick, S. W. (2004) raf RBD and ubiquitin proteins share similar folds, folding rates and mechanisms despite having unrelated amino acid sequences, Biochemistry 43, 8447-8458.
50. Bhatt, A. N., Prakash, K., Subramanya, H. S., and Bhakuni, V. (2002) Different unfolding pathways for mesophilic and thermophilic homologues of serine hydroxymethyltransferase, Biochemistry 41, 12115-12123.
51. DeLano, W. L. (2002) The PyMOL molecular graphics system, DeLano Scientific, San Carlos, CA.