Analysis of long-range structural effects induced by DNase-I interaction with actin monomeric form or complexed to CapZ

Biochimie

Volumn 79, Issue 8, 1997, Pages 485-492

  Usmanova, A ^a   Astier, C ^a   Lebart, M C ^a   Kwiatek, O ^a   Papa, I ^a   Boyer, M ^a   Roustan, C ^a   Benyamin, Y ^a  

^a INSERM   (France)

Author keywords

Actin interaction; Apoptosis; CapZ; DNase I; Split actin

Indexed keywords

ACTIN; CALCIUM ION; CAPZ; CELL PROTEIN; DEOXYRIBONUCLEASE I; ENDONUCLEASE; MAGNESIUM ION; MONOMER; UNCLASSIFIED DRUG;

ARTICLE; BINDING SITE; CAPPING PHENOMENON; CARBOXY TERMINAL SEQUENCE; COMPLEX FORMATION; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; ENZYME ACTIVE SITE; ENZYME CONFORMATION; ENZYME INHIBITION; NONHUMAN; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION;

EID: 0030662160     PISSN: 03009084     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0300-9084(97)82740-X     Document Type: Article

References (52)

1. Mannherz HG, Peitsch MC, Zanotti S, Paddenberg R, Polzar B (1995) A new function for an old enzyme the role of DNase I in apoptosis. Curr Top Microbiol Immunol 198, 161-174
2. Hall AK (1994) Molecular interactions between G-actin DNase I and the beta-thymosins in apoptosis: a hypothesis. Med Hypotheses 43, 125-131
3. Hall AK (1995) Thymosin beta-10 accelerates apoptosis. Cell Mol Biol Res 41, 167-180
4. Polzar B, Zanotti S, Stephan H, Rauch F, Peitsch MC, Irmler M, Tschopp J, Mannherz HG (1994) Distribution of deoxyribonuclease I in rat tissues and its correlation to cellular turnover and apoptosis (programmed cell death). Eur J Cell Biol 64, 200-210
5. Peitsch MC, Irmler M, French LE, Tschopp J (1995) Genomic organisation and expression of mouse deoxyribonuclease I. Biochem Biophys Res Commun 207, 62-68
6. Frankel S, Mooseker MS (1996) The actin-related proteins. Curr Opin Cell Biol 8, 30-37
7. Yonezawa N, Nishida E, Iida K, Yahara I, Sakai H (1990) Inhibition of the interactions of cofilin, destrin, and deoxyribonuclease I with actin by phosphoinositides. J Biol Chem 265, 8382-8386
8. Divecha N, Banfic H, Irvine RF (1991) The polyphosphoinositide cycle exists in the nuclei of Swiss 3T3 cells under the control of a receptor (for IGF-I) in the plasma membrane, and stimulation of the cycle increases nuclear diacylglycerol and apparently induces translocation of protein kinase C to the nucleus. EMBO J 10, 3207-3214
9. Payrastre B, Nievers M, Boonstra J, Breton M, Verkleij AJ, Van Bergen en Henegouwen PM (1992) A differential location of phosphoinositide kinases, diacylglycerol kinase, and phospholipase C in the nuclear matrix. J Biol Chem 267, 5078-5084
10. Sun HQ, Kwiatkowska K, Yin HL (1995) Actin monomer binding proteins. Curr Opin Cell Biol 7, 102-110
11. Jean C, Rieger K, Blanchoin L, Carlier M F, Lenfant M, Pantaloni D (1994). Interaction of G-actin with thymosin beta (4) and its variants thymosin beta (9) and thymosin beta (met) (9). J Muscle Res Cell Motil 15, 278-286
12. Huff T, Zerzawy D, Hannappel E (1995) Interactions of beta-thymosins, thymosin beta 4-sulfoxide and N-terminally truncated thymosin beta 4 with actin studied by equilibrium centrifugation chemical cross-linking and viscometry. Eur J Biochem 230, 650-657
13. McLaughlin PJ, Weeds AG (1995) Actin-binding protein complexes at atomic resolution. Annu Rev Biophys Biomol Struct 24, 643-675
14. Kabsch W, Mannherz HG, Suck D, Pai EF, Holmes KC (1990) Atomic structure of the actin DNase I complex. Nature 347, 37-44
15. Suck D, Oefner C, Kabsch W (1984) Three-dimensional structure of bovine pancreatic DNase I at 2.5 Å resolution. EMBO J 3, 2423-2430
16. Suck D, Lahm A, Oefner C (1988) Structure refined to 2 Å of a nicked DNA octanucleotide complex with DNase I. Nature 332 464-468
17. Weston SA, Lahm A, Suck D (1992) X-ray structure of the DNase I-d (GGTATACC)2 complex at 2.3 Å resolution. J Mol Biol 226, 1237-1256
18. Schutt CE, Myslik JC, Rozycki MD, Goonesekere NCW, Lindberg U (1993) The structure of crystalline profilin-beta-actin. Nature 365, 810-816
19. Tirion MM, ben-Avraham D (1993) Normal mode analysis of G-actin. J Mol Biol 230, 186-195
20. Owen C, Derosier D (1993) A 13-angstrom map of the actin-Scruin filament from the limulus acrosomal process. J Cell Biol 123, 337-344
21. Konno K (1987) Functional chymotryptically split actin and its interaction with myosin subfragment 1. Biochemistry 26, 3582-3589
22. Schwyter D, Phillips M, Reisler E (1989) Subtilisin-cleaved actin polymerization and interaction with myosin subfragment 1. Biochemistry 28, 5889-5895
23. Khaitlina SY, Moraczewska J, Strzeleckagolaszewska H (1993) The actin/actin interactions involving the N-terminus of the DNase-I-Binding loop are crucial for stabilization of the actin filament. Eur J Biochem 218, 911-920
24. Usmanova AM, Khaitlina SY (1989) Protease from a strain of bacteria E coli A2 specifically cleaving actin. Biokhimiya 54, 1308-1314
25. Khaitlina SY, Collins JH, Kuznetsova IM, Pershina VP, Synakevich IG, Turoverov KK, Usmanova AM (1991) Physico-chemical properties of actin cleaved with bacterial protease from E coli A2 strain. FEBS Lett 279, 49-51
26. Sheterline P, Sparrow J (1994) Actin. Protein Profile 1, 1-67
27. Heintz D, Reichert A, Mihelic M, Voelter W, Faulstich H (1993) Use of bimanyl actin derivative (TMB-actin) for studying complexation of β-thymosins. Inhibition of actin polymerization by thymosin β 9. FEBS Lett 329, 9-12
28. (36/32) a barbed end actin-capping protein is a component of the Z-line of skeletal muscle. J Cell Biol 105, 371-379
29. Fowler V (1996) Regulation of actin filament length in erythrocytes and striated muscle. Curr Opin Cell Biol 8, 86-96
30. Ankenbauer T, Kleinschmidt JA, Walsh MJ, Weiner OH, Franke WW (1989) Identification of a widespread nuclear actin binding protein. Nature 342, 822-825
31. Schafer DA, Jennings P, Cooper J (1996) Dynamics of capping protein and actin assembly in vitro uncapping barbed ends by phosphoinositides. J Cell Biol 135, 169-179
32. Hug C, Miller TM, Torres MA, Casella JF, Cooper JA (1992) Identification and characterization of an actin binding site of CapZ. J Cell Biol 116, 923-931
33. Papa I, Kwiatek O, Astier C, Roustan C, Benyamin Y (1997) Purification properties and regulation of CapZ from fish white muscle. J Muscle Res Cell Motil 18, 244
34. Schafer DA, Korshunova YO, Schroer TA, Cooper JA (1994) Differential localisation and sequence analysis of capping protein β-subunit isoforms of vertebrates J Cell Biol 127, 453-465
35. Lebart MC, Méjean C, Boyer M, Roustan C, Benyamin Y (1990) Localization of a new alpha-actinin binding site in the COOH-terminal part of actin sequence. Biochem Biophys Res Commun 207, 62-68
36. Takashi R (1979) Fluorescence energy transfer between subfragment-1 and actin points in the rigor complex of actosubfragment-1. Biochemistry 18, 5164-5169
37. Bayer EA, Wilchek M (1990) Protein biotinylation. Methods Enzymol 184, 138-160
38. Hirs CHW (1967) Reduction and S-carboxymethylation of proteins. Methods Enzymol 11, 199-204
39. 2+ on actin monomers. An immunologic attempt to localize the affected region. FEBS Lett 181, 119-123
40. Labbé JP, Méjean C, Benyamin Y, Roustan C (1990) Characterization of an actin-myosin head interface in the 40-113 region of actin using specific antigenic probes. Biochem J 271, 407-413
41. Casella JF, Cooper JA (1991) Purification of CapZ from chick skeletal muscle. Methods Enzymol 193, 140-154
42. Labbé JP, Boyer M, Méjean C, Roustan C, Benyamin Y (1993) Localization of two myosin-subfragment-1 binding contacts in the 96-132 region of actin subdomain-1. Eur J Biochem 215, 17-24
43. Laemmli JO (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685
44. Boyer M, Roustan C, Benyamin Y (1985) DNase I-actin complex an immunologic study. Biosci Rep 5, 69-46
45. Drewes G, Faulstich H (1991) A reversible conformational transition in muscle actin is caused by nucleotide exchange and uncovers cysteine in position 10. J Biol Chem 266, 5508-5513
46. Kabsch W, Vandekerckhove J (1992) Structure and function of actin. Annu Rev Biophys Struct 21, 49-76
47. Frieden C, Lieberman D, Gilbert HR (1980) A fluorescent probe for conformational changes in skeletal muscle G-actin. J Biol Chem 255, 8991-8993
48. Ajtai K, Venyaminov S (1983) CD study of the actin DNase I complex. FEBS Lett 151, 94-96
49. Miki M, Walsh MP, Hartshorne DJ (1992) The mechanism of inhibition of the actin-activated myosin Mg-ATPase by calponin. Biochem Biophys Res Commun 187, 867-871
50. Bertazzon A, Tian GH, Lamblin A, Tsong TY (1990) Enthalpic and entropic contributions to actin stability calorimetry circular dichroism and fluorescence study and effects of calcium. Biochemistry 29, 291-298
51. Casella JF, Torres MA (1994) Interaction of Cap Z with actin. The NH2-Terminal domains of the alpha 1 and beta subunits are not required for actin capping and alpha 1 beta and alpha 2 beta heterodimers bind differentially to actin. J Biol Chem 269, 6992-6998
52. Kuznetsova I, Antropova O, Turoverov K, Khaitlina S (1996) Conformational changes in subdomain I of actin induced by proteolytic cleavage within the DNase I-binding loop: energy transfer from tryptophan to AEDANS. FEBS Lett 383, 105-108