Autoproteolysis of rat p67 generates several peptide fragments: The N-terminal fragment, p26, is required for the protection of eIF2α from phosphorylation

Biochemistry

Volumn 46, Issue 11, 2007, Pages 3465-3475

  Datta, Bansidhar ^a   Ghosh, Arnab ^a   Majumdar, Avijit ^a   Datta, Rekha ^a  

^a KENT STATE UNIVERSITY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

APROTININ; CATION EXCHANGE CHROMATOGRAPHY; EUKARYOTIC INITIATION FACTOR; RAT P67;

AMINO ACIDS; BIOCHEMISTRY; CELL GROWTH; MOLECULAR SIEVES; PEPTIDES; PHOSPHORYLATION;

PROTEINS;

APROTININ; BESTATIN; INITIATION FACTOR 2ALPHA; LEUPEPTIN; MUTANT PROTEIN; N [N (3 CARBOXYOXIRANE 2 CARBONYL)LEUCYL]AGMATINE; POTASSIUM ION; PROTEIN P26; PROTEIN P52; PROTEIN P67; PROTEIN SUBUNIT; PROTEINASE INHIBITOR; RECOMBINANT PROTEIN; SERINE PROTEINASE INHIBITOR; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ANION EXCHANGE; ARTICLE; BACULOVIRUS; CELL GROWTH; CELL PROLIFERATION; CONTROLLED STUDY; FRACTIONATION; GENETIC TRANSFECTION; ION EXCHANGE CHROMATOGRAPHY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN DOMAIN; PROTEIN PHOSPHORYLATION; RAT; REGULATORY MECHANISM;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; AMINOPEPTIDASES; ANIMALS; CELLS, CULTURED; EIF-2 KINASE; EUKARYOTIC INITIATION FACTOR-2; GLYCOPROTEINS; MICE; PEPTIDE FRAGMENTS; PEPTIDE HYDROLASES; PHOSPHORYLATION; PROTEASE INHIBITORS; RATS; RECOMBINANT PROTEINS;

EUKARYOTA; HEXAPODA; MAMMALIA; RATTUS;

EID: 33947375702     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi061838n     Document Type: Article

References (43)

1. Merrick, W. C., and Hershey, J. W. B. (2000) Pathway and mechanism of initiation of protein synthesis, in Translational control in gene expression (Hershey, J. W. B., Mathews, M. B., and Sonenberg, N., Eds.) pp 33-88, Cold Spring Harbor Laboratory Press, Plainview, NY.
2. Datta, B., Chakrabarti, D., Roy, A. L., and Gupta, N. K. (1988) Roles of a 67 kDa polypeptide in protein synthesis inhibition in heme-deficient reticulocyte lysates, Proc. Natl. Acad. Sci. U.S.A. 85, 3324-3328.
3. Ghosh, A., Datta, R., Majumdar, A., Bhattacharya, M., and Datta, B. (2006) The N-terminal lysine residue-rich domain II and the 340-430 amino acid segment of eukaryotic initiation factor 2-associated glycoprotein p67 are the binding sites for the γ-subunit of eIF2, Exp. Cell Res. 312, 3184-3203.
4. Ray, M. K., Chakraborty, A., Datta, B., Chattopadyay, A., Saha, D., Bose, A., Kinzy, T. G., Hileman, R. E., Merrick, W. C., and Gupta, N. K. (1993) Characterization of the eukaryotic initiation factor 2 associated 67-kDa polypeptide, Biochemistry 32, 5151-5159.
5. Bose, A., Saha, D., and Gupta, N. K. (1997) Viral infection: I. Regulation of protein synthesis during vaccinia viral infection of animal cells, Arch. Biochem. Biophys. 342, 362-372.
6. Datta, B. (2000) MAPs and POEP of the roads from prokaryotic to eukaryotic kingdoms, Biochimie 82, 95-107.
7. Datta, B., Datta, R., Ghosh, A., and Majumdar, A. (2004) Eukaryotic initiation factor 2-associated glycoprotein, p67, shows differential effects on the activity of certain kinases during serum-starved conditions, Arch. Biochem. Biophys. 427, 68-78.
8. Datta, B., Datta, R., Ghosh, A., and Majumdar, A. (2006) The binding between p67 and eukaryotic initiation factor 2 plays important roles in the protection of eIF2α from phosphorylation by kinases, Arch. Biochem. Biophys. 452, 138-148.
9. 2/M boundary in human osteosarcoma cells correlates with deglycosylation of p67 and a decreased rate of protein synthesis, Exp. Cell Res. 250, 223-230.
10. 67) and its possible role in the inhibition of eIF-2 kinase-catalyzed phosphorylation of the eIF-2α-subunit, J. Biol Chem. 264, 20620-20624.
11. Datta, B., Ray, M. K., Chakrabarti, D., and Gupta, N. K. (1988) Roles of eIF-2 and eIF-2-associated protein in regulation of protein synthesis during growth of animal cells in culture, Indian J. Biochem. Biophys. 25, 478-482.
12. Datta, R., Tammali, R., and Datta, B. (2003) Negative regulation of the protection of eIF2α phosphorylation activity by a unique acidic domain present at the N-terminus of p67, Exp. Cell Res. 283, 237-246.
13. Gupta, S., Bose, A., Chatterjee, N., Saha, D., Wu, S., and Gupta, N. K. (1997) p67 transcription regulates translation in serum-starved and mitogen-activated KRC-7 cells, J. Biol. Chem. 272, 12699-12704.
14. 67) and its requirement in protein synthesis, Gene Expression 5, 113-122.
15. Ray, M. K., Datta, B., Chakrabarti, A., Chattopadhyay, A., Meza-Keuthan, S., and Gupta, N. K. (1992) The eukaryotic initiation factor 2-associated 67-kDa polypeptide (p67) plays a critical role in regulation of protein synthesis initiation in animal cells, Proc. Natl. Acad. Sci. U.S.A. 89, 539-543.
16. Saha, D., Wu, S., Bose, A., Chatterjee, N., Chakraborty, A., Chatterjee, M., and Gupta, N. K. (1997) Viral infection: II. Hemin induces overexpression of p67 as it partially prevents appearance of an active p67-deglycosylase in baculovirus-infected insect cells, Arch. Biochem. Biophys. 342, 373-382.
17. Wu, S., Rehemtulla, A., Gupta, N. K., and Kaufman, R. J. (1996) A eukaryotic translational initiation factor 2-associated 67 kDa glycoprotein partially reverses protein synthesis initiation by activated double-stranded RNA-dependent protein kinase in intact cells, Biochemistry 35, 8275-8280.
18. Cutforth, T., and Gaul, U. A. (1999) Methionine aminopaptidase and putative regulator of translation initiation is required for cell growth and patterning in Drosophila, Mech. Dev. 82, 23-28.
19. Klinkenberg, M., Ling, C., and Chang, Y. H. (1997) A dominant negative mutation in Saccharomyces cerevisiae methionine aminopeptidase-1 affects catalysis and interferes with the function of methionine aminopeptidase-2, Arch. Biochem. Biophys. 347, 193-200.
20. Kwon, J.-Y., Jeong, H. W., Kim, H. K., Kang, K. H., Chang, Y. H., Bae, K. S., Choi, J. D., Lee, U. C., Son, K. H., and Kwon, B. M. (2000) cis-Fumagillin, a new methionine aminopeptidase (type 2) inhibitor produced by penicillium sp. F2757, J. Antibiot. 53, 799-806.
21. 67), Biochim. Biophys. Acta 1260, 333-336.
22. Li, X., and Chang, Y. H. (1995) Amino-terminal protein processing in Saccharomyces cerevisiae is an essential function that requires two distinct methionine aminopeptidases, Proc. Natl. Acad. Sci. U.S.A. 92, 2357-2361.
23. 67), J. Biol. Chem. 268, 10796-10801.
24. Zhang, P., Nicholson, D. E., Bujnicki, J. M., Su, X., Brendle, J. J., Fredig, M., Kyle, D. E., Milhous, W. K., and Chiang, P. K. (2002) Angiogenesis inhibitors specific for methionine aminopeptidase 2 as drugs for malaria and leishmaniasis, J. Biomed. Sci. 9, 34-40.
25. Datta, R., Choudhury, P., Bhattacharya, M., Leon, F. S., Zhou, Y., and Datta, B. (2001) Protection of translation initiation factor eIF2 phosphorylation correlates with eIF2-associated glycoprotein p67 levels and requires the lysine-rich domain I of p67, Biochimie 83, 919-931.
26. 63 of p67 is required for its ability to regulate the phosphorylation and activity of eukaryotic initiation factor 2α, Biochemistry 42, 5453-5460.
27. Bazan, J. F., Weaver, L. H., Roderick, S. L., Huber, R., and Matthews, B. W. (1993) Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold, Proc. Natl. Acad. Sci. U.S.A. 91, 2473-2477.
28. Keeling, P. J., and Doolittle, W. F. (1996) Methionine aminopeptidase-1: The MAP of the mitochondrion? Trends Biochem. Sci. 21, 285-286.
29. Liu, S., Widom, J., Kemp, C. W., Crews, C. M., and Clardy, J. (1998) Structure of human methionine aminopeptidase-2 complexed with fumagillin, Science 282, 1324-1327.
30. Arfin, S. M., Kendall, R. L., Hall, L., Weaver, L. H., Stewart, A. E., Matthews, B. W., and Bradshaw, R. A. (1995) Eukaryotic methionyl aminopeptidases: Two classes of cobalt-dependent enzymes, Proc. Natl. Acad. Sci. U.S.A. 92, 7714-7718.
31. Zuo, S., Guo, Q., Ling, C., and Chang, Y. H. (1995) Evidence that two zinc fingers in the methionine aminopeptidase from Saccharomyces cerevisiae is important for normal growth, Mol. Gen. Genet. 246, 247-253.
32. Yang, G., Kirkpatrick, R. B., Ho, T., Zhang, G.-F., Liang, P.-H., Johanson, K. O., Casper, D. J., Doyle, M. L., Marino, J. P., Jr., Thompson, S. K., Chen, W., Tew, D. G., and Meek, T. D. (2001) Steady-state kinetic characterization of substrates and metal-ion specificities of the full-length and N-terminally truncated recombinant human methionine aminopeptidase (type 2), Biochemistry 40, 10645-10654.
33. 2+ as a cofactor: A case of mistaken identity? Protein Sci. 7, 2684-2687.
34. Walker, K. W., and Bradshaw, R. A. (1999) Yeast methionine aminopeptidase I. Alteration of substrate specificity by site-directed mutagenesis, J. Biol. Chem. 274, 13403-13409.
35. Wang, J., Sheppard, G. S., Lou, P., Kawai, M., Park, C., Egan, D. A., Schneider, A., Bouska, J., Lesniewski, R., and Henkin, J. (2003) Physiological relevant metal cofactor for methionine aminopeptidase 2 is manganese, Biochemistry 42, 5035-5042.
36. Datta, B., Datta, R., Ghosh, A., and Majumdar, A. (2004) The stability of eukaryotic initiation factor 2-associated glycoprotein, p67, and that inhibits the phosphorylation of extracellular signal-regulated kinases 1 and 2, Exp. Cell Res. 303, 174-182.
37. Griffith, E. C., Su, Z., Niwayama, S., Ramsay, C. A., Chang, Y.-W., Wu, Z., and Liu, J. O. (1997) Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2, Proc. Natl. Acad. Sci. U.S.A. 95, 15183-15188.
38. Griffith, E. C., Su, Z., Turk, B. E., Chen, S., Chang, Y. W., Wu, Z., Biemann, K., and Liu, J. O. (1997) Methionine aminopeptidase (type 2) is the common target for angiogenesis inihibitors AGM-14470 and ovalicin, Chem. Biol. 4, 461-471.
39. Datta, B., Datta, R., Majumdar, A., and Balusu, R. (2004) Treatment of cells with the angiogenic inhibitor fumagillin results in increased stability of eukaryotic initiation factor 2-associated glycoprotein, p67, and reduced phosphorylation of extracellular signal-regulated kinases 1 and 2, Biochemistry 43, 14821-14831.
40. Sakamoto, K. M., Kim, K. B., Kumagali, A., Mercurio, F., and Crews, C. M. (2001) Protacs: Chimeric molecules that target proteins to the Skp1-Cullin-F box complex for ubiquitination and degradation, Proc. Natl. Acad. Sci. U.S.A. 98, 8554-8559.
41. Neurath, H. (1999) Proteolytic enzymes, past and future, Proc. Natl. Acad. Sci. U.S.A. 96, 10962-10963.
42. Lampi, K. J., Amyx, K. K., Ahmann, P., and Steel, E. A. (2006) Deamidation in human lens βB2-crystallin destabilizes the dimer, Biochemistry 45, 3146-3153.
43. Nonato, M. C., Widom, J., and Clardy, J. (2002) Crystal structure of the N-terminal segment of human eukaryotic translation initiation factor 2α, J. Biol. Chem. 277, 17057-17061.