Cloning, bacterial expression, and unique structure of adenosylhomocysteine hydrolase-like protein 1, or inositol 1,4,5-triphosphate receptor-binding protein from mouse kidney

Biochimica et Biophysica Acta - Proteins and Proteomics

Volumn 1784, Issue 11, 2008, Pages 1786-1794

  Gomi, Tomoharu ^a   Takusagawa, Fusao ^b   Nishizawa, Mikio ^c   Bukhari, Agussalim ^a   Usui, Isao ^a   Sugiyama, Eiji ^a   Taki, Hirofumi ^a   Shinoda, Kouichiro ^a   Hounoki, Hiroyuki ^a   Miwa, Toshiro ^a   Tobe, Kazuyuki ^a   Kobayashi, Masashi ^a   Ishimoto, Tetsuya ^a   Ogawa, Hirofumi ^a   Mori, Hisashi ^a  

^a UNIVERSITY OF TOYAMA   (Japan)

^b UNIVERSITY OF KANSAS   (United States)

^c RITSUMEIKAN UNIVERSITY   (Japan)

Author keywords

Inositol 1,4,5 triphosphate receptor binding protein; IRBIT; NAD+ binding; S adenosylhomocysteine hydrolase like protein; SAH L

Indexed keywords

ADENOSYLHOMOCYSTEINASE; ADENOSYLHOMOCYSTEINE HYDROLASE LIKE PROTEIN 1; COMPLEMENTARY DNA; INOSITOL 1,4,5 TRIPHOSPHATE RECEPTOR BINDING PROTEIN; INOSITOL 1,4,5 TRISPHOSPHATE RECEPTOR; NICKEL; NICOTINAMIDE ADENINE DINUCLEOTIDE; POLYHISTIDINE TAG; PROTEIN; PROTEINASE; TRYPSIN; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; BINDING AFFINITY; CARBOXY TERMINAL SEQUENCE; CIRCULAR DICHROISM; CONTROLLED STUDY; CROSS LINKING; DNA ISOLATION; DNA SEQUENCE; ENZYME ACTIVITY; ENZYME BINDING; ESCHERICHIA COLI; GEL FILTRATION; MOLECULAR CLONING; MOUSE; NONHUMAN; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA;

EID: 55549095981     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2008.08.016     Document Type: Article

References (29)

1. Dekker J.W., Budhia S., Angel N.Z., Cooper B.J., Clark G.J., Hart D.N.J., and Kato M. Identification of an S-adenosylhomocysteine hydrolase-like transcript induced during dendritic cell differentiation. Immunogenetics 53 (2002) 993-1001
2. Cooper B.J., Key B., Carter A., Angel N.Z., Hart D.N.J., and Kato M. Suppression and overexpression of adenosylhomocysteine hydrolase-like protein 1 (AHCYL1) influences zebrafish embryo development. A possible role for AHCYL1 in inositol phospholipid signaling. J. Biol. Chem. 281 (2006) 22471-22484
3. 3 binding to the receptor. J. Biol. Chem. 278 (2003) 10602-10612
4. 3 receptor. Mol. Cell 22 (2006) 795-806
5. - cotransporter 1 (pNBC1). Proc. Natl. Acad. Sci. U. S. A. 103 (2006) 9542-9547
6. Devogelaere B., Kasri N.N., Derua R., Waelkens E., Callewaert G., Missiae L., Parys J.B., and Smedt H.D. Binding of IRBIT to the IP3 receptor. Determinants and functional effects. Biochem. Biophys. Res. Commun. 343 (2006) 49-56
7. Devogelaere B., Beullens M., Sammels E., Derua R., Waelkens E., Lint J.V., Parys J.B., Missiaen L., Bollen M., and Smedt H.D. Protein phosphatase-1 is a novel regulator of the interaction between IRBIT and the inositol 1,4,5-trisphosphate receptor. Biochem. J. 407 (2007) 303-311
8. 2+ channel. From discovery to new signaling concepts. J. Neurochem. 102 (2007) 1426-1446
9. Dela Haba G., and Cantoni G.L. The enzymatic synthesis of S-adenosyl-l-homocysteine from adenosine and homocysteine. J. Biol. Chem. 234 (1959) 603-608
10. Miller M.W., Duhl D.M., Winkes B.M., Arredondo-Vega F., Saxon P.J., Wolff G.L., Hershfield M.S., and Barsh G.S. The mouse lethal nonagouti (a(x)) mutation deletes the S-adenosylhomocysteine hydrolase (Ahcy) gene. EMBO J. 13 (1994) 1806-1816
11. Palmer J.L., and Abeles R.H. Mechanism of bovine liver S-adenosylhomocysteine hydrolase. Steady-state and pre-steady-state kinetic analysis. J. Biol. Chem. 251 (1976) 5817-5819
12. Palmer J.L., and Abeles R.H. The mechanism of action of S-adenosylhomocysteinase. J. Biol. Chem. 254 (1979) 1217-1226
13. Fujioka M., and Takata Y. S-Adenosylhomocysteine hydrolase from rat liver. Purification and some properties. J. Biol. Chem. 256 (1981) 1631-1635
14. Gomi T., and Fjioka F. S-Adenosylhomocysteinase from rat liver. Evidence for structurally identical and catalytically equivalent subunits. J. Biol. Chem. 260 (1985) 2789-2793
15. Ogawa H., Gomi T., Mueckler M.M., Fujioka M., Backlund Jr. P.S., Aksamit R.R., Unson C.G., and Cantoni G.L. Amino acid sequence of S-adenosyl-l-homocysteine hydrolase from rat liver as derived from the cDNA sequence. Proc. Natl. Acad. Sci. U. S. A. 84 (1987) 719-723
16. Gomi T., Date T., Ogawa H., Fujioka M., Aksamit R.R., Backlund Jr. P.S., and Cantoni G.L. Expression of rat liver S-adenosylhomocysteinase cDNA in Escherichia coli and mutagenesis at the putative NAD binding site. J. Biol. Chem. 264 (1989) 16138-16142
17. Gomi T., Takata Y., Date T., Fujioka M., Aksamit R.R., Backlund Jr. P.S., and Cantoni G.L. Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding. J. Biol. Chem. 265 (1990) 16102-16107
18. Hu Y., Komoto J., Huang T., Gomi T., Ogawa H., Takata Y., Fujioka M., and Takusagawa F. Crystal structure of S-adenosylhomocysteine hydrolase from rat liver. Biochemistry 38 (1999) 8323-8333
19. Takata Y., Yamada T., Huang Y., Komoto J., Gomi T., Ogawa H., Fujioka M., and Takusagawa F. Catalytic mechanism of S-adenosylhomocysteine hydrolase. Site-directed mutagenesis of Asp-130, Lys-185, Asp-189, and Asn-190. J. Biol. Chem. 277 (2002) 22670-22676
20. Chomczynski P., and Sacchi N. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162 (1987) 156-159
21. Davies G.E., and Stark G.R. Use of dimethyl suberimidate, a cross-linking reagent, in studying the subunit structure of oliogmeric proteins. Proc. Natl. Ada. Sci. U. S. A. 66 (1970) 651-656
22. Weber K., and Osborn M. The reliability of molecular weight determinations by dodecyl sulfate-polyacrylamide gel electrophoresis. J. Biol. Chem. 244 (1969) 4406-4412
23. Lowry O.H., Rosebrugh N.J., Farr A.L., and Randall R.J. Protein measurement with the Folin phenol reagent. J. Biol. Chem. 193 (1951) 265-275
24. Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
25. Chou P.Y., and Fasman G.D. Prediction of the secondary structure of proteins from their amino acid sequence. Adv. Enzymol Relat. Areas Mol. Biol. 45 (1978) 1-45
26. Rossmann M.G. Comparison of the evolution of heme binding and NAD binding proteins. Fed. Proc. 35 (1976) 2112-2114
27. Chen Y.H., Yang J.T., and Martinez H.M. Determination of the secondary structures of proteins by circular dichroism and optical rotatory dispersion. Biochemistry 11 (1972) 4120-4131
28. Gomi T., Takata Y., Date T., Fujioka M., Aksamit R.R., Backlund Jr. P.S., and Cantoni G.L. Site-directed mutagenesis of rat liver S-adenosylhomocysteinase. Effect of conversion of aspartic acid 244 to glutamic acid on coenzyme binding. J. Biol. Chem. 265 (1990) 16102-16107
29. 4. Hybridization in the purification of lactate dehydrogenase isozymes. J. Biol. Chem. 249 (1974) 4961-4968