Purification and characterization of pepsins A1 and A2 from the Antarctic rock cod Trematomus bernacchii

FEBS Journal

Volumn 274, Issue 23, 2007, Pages 6152-6166

  Brier, Sébastien ^a   Maria, Giovanna ^b   Carginale, Vincenzo ^b   Capasso, Antonio ^b   Wu, Yan ^a   Taylor, Robert M ^a   Borotto, Nicholas B ^a   Capasso, Clemente ^b   Engen, John R ^a  

^a NORTHEASTERN UNIVERSITY   (United States)

^b INSTITUTE OF PROTEIN BIOCHEMISTRY   (Italy)

Author keywords

Aspartic proteases; Cold adapted protein; Rock cod; Specificity

Indexed keywords

PEPSIN A; PEPSIN A1; PEPSIN A2; PEPSTATIN; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; ATLANTIC COD; BIOPHYSICS; CLONE; CONTROLLED STUDY; ESCHERICHIA COLI; GENE DUPLICATION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PURIFICATION; STOMACH PH; SWINE; TEMPERATURE SENSITIVITY; TREMATOMUS BERNACCHII;

AMINO ACID SEQUENCE; ANIMALS; ANTARCTIC REGIONS; BINDING SITES; CLONING, MOLECULAR; ENZYME PRECURSORS; ENZYME STABILITY; ESCHERICHIA COLI; GASTRIC MUCOSA; HYDROGEN-ION CONCENTRATION; INCLUSION BODIES; ISOENZYMES; KINETICS; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MOLECULAR WEIGHT; PEPSIN A; PEPSTATINS; PERCIFORMES; PROTEASE INHIBITORS; PROTEIN BINDING; PROTEIN FOLDING; PROTEIN STRUCTURE, SECONDARY; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SOLUBILITY; SUBSTRATE SPECIFICITY; SWINE; TEMPERATURE;

ESCHERICHIA COLI; LOTELLA RHACINA; SEBASTES SCHLEGELI; SUIDAE; SUS; TREMATOMUS BERNACCHII;

EID: 36248995763     PISSN: 1742464X     EISSN: 17424658     Source Type: Journal    
DOI: 10.1111/j.1742-4658.2007.06136.x     Document Type: Article

References (43)

1. Brodeur JC, Calvo J, Clarke A Johnston IA (2003) Myogenic cell cycle duration in Harpagifer species with sub-Antarctic and Antarctic distributions: evidence for cold compensation. J Exp Biol 206, 1011 1016.
2. Chen L, DeVries AL Cheng CH (1997) Evolution of antifreeze glycoprotein gene from a trypsinogen gene in Antarctic notothenioid fish. Proc Natl Acad Sci USA 94, 3811 3816.
3. Detrich HW 3rd (1997) Microtubule assembly in cold-adapted organisms: functional properties and structural adaptations of tubulins from antarctic fishes. Comp Biochem Physiol A Physiol 118, 501 513.
4. D'Avino R, Caruso C, Camardella L, Schninà ME, Rutigliano B, Romano M, Carratore V, Barra D di Prisco G (1991) An Overwiew of the Molecular Structure and Funtional Properties of the Hemoglobins of a Cold-Adapted Antarctic Teleost. Springer-Verlag, Berlin.
5. Kageyama T (2002) Pepsinogens, progastricsins, and prochymosins: structure, function, evolution, and development. Cell Mol Life Sci 59, 288 306.
6. Kageyama T, Ichinose M, Miki K, Athauda SB, Tanji M Takahashi K (1989) Difference of activation processes and structure of activation peptides in human pepsinogens A and progastricsin. J Biochem (Tokyo) 105, 15 22.
7. Fusek M Vetvicka V (1995) Aspartic Proteinases. Physiology and Pathology. CRC Press, Boca Raton.
8. 2)Phe-Arg-Leu, by selected aspartic proteinases: evidence for specific interactions in subsites S3 and S2. Biochim Biophys Acta 913, 122 130.
9. Fruton JS (1970) The specificity and mechanism of pepsin action. Adv Enzymol Relat Areas Mol Biol 33, 401 443.
10. Foltmann B (1981) Gastric proteinases: structure, function, evolution and mechanism of action. Essays Biochem 17, 52 84.
11. Abad-Zapatero C, Rydel TJ Erickson J (1990) Revised 2,3, a structure of porcine pepsin: evidence for a flexible subdomain. Proteins 8, 62 81.
12. Fujinaga M, Chernaia MM, Tarasova NI, Mosimann SC James MN (1995) Crystal structure of human pepsin and its complex with pepstatin. Protein Sci 4, 960 972.
13. Gildberg A, Olsen RL Bjarnason JB (1990) Catalytic properties and chemical composition of pepsins from Atlantic cod (Gadus morhua). Comp Biochem Physiol B 96, 323 330.
14. Sanchez LM, Freije JP, Merino AM, Vizoso F, Foltmann B Lopez-Otin C (1992) Isolation and characterization of a pepsin C zymogen produced by human breast tissues. J Biol Chem 267, 24725 24731.
15. Gildberg A (1988) Aspartic proteinases in fishes and acquatic invertebrates. Comp Biochem Physiol B 91, 425 435.
16. Tanji M, Kageyama T Takahashi K (1988) Tuna pepsinogens and pepsins. Purification, characterization and amino-terminal sequences. Eur J Biochem 177, 251 259.
17. Carginale V, Trinchella F, Capasso C, Scudiero R, Riggio M Parisi E (2004) Adaptive evolution and functional divergence of pepsin gene family. Gene 333, 81 90.
18. Marshall CJ (1997) Cold-adapted enzymes. Trends Biotechnol 15, 359 364.
19. Lin XL, Wong RN Tang J (1989) Synthesis, purification, and active site mutagenesis of recombinant porcine pepsinogen. J Biol Chem 264, 4482 4489.
20. Cooper JB, Khan G, Taylor G, Tickle IJ Blundell TL (1990) X-ray analyses of aspartic proteinases. II. Three-dimensional structure of the hexagonal crystal form of porcine pepsin at 2.3 A resolution. J Mol Biol 214, 199 222.
21. Sielecki AR, Fedorov AA, Boodhoo A, Andreeva NS James MN (1990) Molecular and crystal structures of monoclinic porcine pepsin refined at 1.8 A resolution. J Mol Biol 214, 143 170.
22. Marciniszyn J Jr., Hartsuck JA Tang J (1976) Mode of inhibition of acid proteases by pepstatin. J Biol Chem 251, 7088 7094.
23. Fujinaga M, Cherney MM, Tarasova NI, Bartlett PA, Hanson JE James MN (2000) Structural study of the complex between human pepsin and a phosphorus-containing peptidic-transition-state analog. Acta Crystallogr D Biol Crystallogr 56, 272 279.
24. Genicot S, Rentier-Delrue F, Edwards D, VanBeeumen J Gerday C (1996) Trypsin and trypsinogen from an Antarctic fish: molecular basis of cold adaptation. Biochim Biophys Acta 1298, 45 57.
25. Cheng CH Detrich WH (2007) Molecular ecophysiology of Antarctic notothenioid fishes. Phil Trans R Soc Lond B Biol Sci B362, 1 18.
26. D'Amico S, Claverie P, Collins T, Georlette D, Gratia E, Hoyoux A, Meuwis MA, Feller G Gerday C (2002) Molecular basis of cold adaptation. Phil Trans R Soc Lond B Biol Sci 357, 917 925.
27. Foltmann B (1981) Gastric proteinases - structure, function, evolution and mechanism of action. Essays Biochem 17, 52 84.
28. Zelle B, Evers MP, Groot PC, Bebelman JP, Mager WH, Planta RJ, Pronk JC, Meuwissen SG, Hofker MH, Eriksson AW et al. (1988) Genomic structure and evolution of the human pepsinogen A multigene family. Hum Genet 78, 79 82.
29. Lu Q, Wolfe KH McConnell DJ (1988) Molecular cloning of multiple bovine aspartyl protease genes. Gene 71, 135 146.
30. Kageyama T (2000) New world monkey pepsinogens A and C, and prochymosins. Purification, characterization of enzymatic properties, cDNA cloning, and molecular evolution. J Biochem (Tokyo) 127, 761 770.
31. Feller G, Narinx E, Arpigny JL, Aiattaleb M, Daise E, Genicot S Gerday C (1996) Enzymes from psycrophilic organisms. FEMS Microbiol Rev 18, 189 202.
32. Feller G, Payan F, Theys F, Qian M, Haser R Gerday C (1994) Stability and structural analysis of alpha-amylase from the antarctic psychrophile Alteromonas haloplanctis A23. Eur J Biochem 222, 441 447.
33. Keil B (1992) Specificity of Proteolysis. Springer-Verlag, Berlin.
34. Shintani T, Nomura K Ichishima E (1997) Engineering of porcine pepsin. Alteration of S1 substrate specificity of pepsin to those of fungal aspartic proteinases by site-directed mutagenesis. J Biol Chem 272, 18855 18861.
35. Yang JT, Wu CS Martinez HM (1986) Calculation of protein conformation from circular dichroism. Methods Enzymol 130, 208 269.
36. Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680 685.
37. Matsudaira P (1987) Sequence from picomole quantities of proteins electroblotted onto polyvinylidene difluoride membranes. J Biol Chem 262, 10035 10038.
38. Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72, 248 254.
39. Gasteiger E, Gattiker A, Hoogland C, Ivanyi I, Appel RD Bairoch A (2003) ExPASy: the proteomics server for in-depth protein knowledge and analysis. Nucleic Acids Res 31, 3784 3788.
40. Dame JB, Reddy GR, Yowell CA, Dunn BM, Kay J Berry C (1994) Sequence, expression and modeled structure of an aspartic proteinase from the human malaria parasite Plasmodium falciparum. Mol Biochem Parasitol 64, 177 190.
41. Dunn BM, Jimenez M, Parten BF, Valler MJ, Rolph CE Kay J (1986) A systematic series of synthetic chromophoric substrates for aspartic proteinases. Biochem J 237, 899 906.
42. Higgins DG Sharp PM (1988) CLUSTAL: a package for performing multiple sequence alignment on a microcomputer. Gene 73, 237 244.
43. Rao JK, Bujacz G Wlodawer A (1998) Crystal structure of rabbit muscle creatine kinase. FEBS Lett 439, 133 137.