The carboxyl-terminal region of erythroid-specific 5-aminolevulinate synthase acts as an intrinsic modifier for its catalytic activity and protein stability

Experimental Hematology - Tập 40 - Trang 477-486.e1 - 2012
Senkottuvelan Kadirvel1, Kazumichi Furuyama1, Hideo Harigae2, Kiriko Kaneko3, Yoshiko Tamai4, Yoji Ishida5, Shigeki Shibahara1
1Department of Molecular Biology and Applied Physiology, Tohoku University School of Medicine, Sendai, Japan
2Department of Hematology and Rheumatology, Tohoku University School of Medicine, Sendai, Japan
3Endocrinology and Applied Medical Science, Tohoku University School of Medicine, Sendai, Japan
4Division of Transfusion Medicine, Hirosaki University Hospital, Hirosaki, Japan
5Hematology and Oncology, Internal Medicine, Iwate Medical University School of Medicine, Morioka, Japan

Tài liệu tham khảo

Anderson, 2001, Disorders of heme biosynthesis: X-linked sideroblastic anemia and the porphyrias, 2991 Hayashi, 1970, Difference in molecular sizes of delta-aminolevulinate synthetases in the soluble and mitochondrial fractions of rat liver, J Biochem, 67, 859, 10.1093/oxfordjournals.jbchem.a129319 Bishop, 1990, Human delta-aminolevulinate synthase: assignment of the housekeeping gene to 3p21 and the erythroid-specific gene to the X chromosome, Genomics, 7, 207, 10.1016/0888-7543(90)90542-3 Lathrop, 1993, Regulation by heme of mitochondrial protein transport through a conserved amino acid motif, Science, 259, 522, 10.1126/science.8424176 Munakata, 2004, Role of the heme regulatory motif in the heme-mediated inhibition of mitochondrial import of 5-aminolevulinate synthase, J Biochem, 136, 233, 10.1093/jb/mvh112 Dailey, 2005, Examination of mitochondrial protein targeting of haem synthetic enzymes: in vivo identification of three functional haem-responsive motifs in 5-aminolaevulinate synthase, Biochem J, 386, 381, 10.1042/BJ20040570 Munakata, 1993, Purification and structure of rat erythroid-specific delta-aminolevulinate synthase, J Biochem, 114, 103, 10.1093/oxfordjournals.jbchem.a124123 Cox, 1990, Erythroid 5-aminolevulinate synthase is located on the X chromosome, Am J Hum Genet, 46, 107 Cox, 1994, X-linked pyridoxine-responsive sideroblastic anemia due to a Thr388-to-Ser substitution in erythroid 5-aminolevulinate synthase, N Engl J Med, 330, 675, 10.1056/NEJM199403103301004 Cotter, 1992, Enzymatic defect in “X-linked” sideroblastic anemia: molecular evidence for erythroid delta-aminolevulinate synthase deficiency, Proc Natl Acad Sci U S A, 89, 4028, 10.1073/pnas.89.9.4028 Whatley, 2008, C-terminal deletions in the ALAS2 gene lead to gain of function and cause X-linked dominant protoporphyria without anemia or iron overload, Am J Hum Genet, 83, 408, 10.1016/j.ajhg.2008.08.003 Bottomley, 2009, Sideroblastic anemias, 835 Harigae, 2010, Hereditary sideroblastic anemia: pathophysiology and gene mutations, Int J Hematol, 92, 425, 10.1007/s12185-010-0688-4 Ducamp, 2011, Sideroblastic anemia: molecular analysis of the ALAS2 gene in a series of 29 probands and functional studies of 10 missense mutations, Hum Mutat, 32, 590, 10.1002/humu.21455 Harigae, 1999, A novel mutation of the erythroid-specific delta-aminolaevulinate synthase gene in a patient with X-linked sideroblastic anaemia, Br J Haematol, 106, 175, 10.1046/j.1365-2141.1999.01479.x Cazzola, 2002, Absent phenotypic expression of X-linked sideroblastic anemia in one of 2 brothers with a novel ALAS2 mutation, Blood, 100, 4236, 10.1182/blood-2002-03-0685 Astner, 2005, Crystal structure of 5-aminolevulinate synthase, the first enzyme of heme biosynthesis, and its link to XLSA in humans, EMBO J, 24, 3166, 10.1038/sj.emboj.7600792 To-Figueras, 2011, ALAS2 acts as a modifier gene in patients with congenital erythropoietic porphyria, Blood, 118, 1443, 10.1182/blood-2011-03-342873 Sambrook, 2001 Furuyama, 1997, Pyridoxine refractory X-linked sideroblastic anemia caused by a point mutation in the erythroid 5-aminolevulinate synthase gene, Blood, 90, 822, 10.1182/blood.V90.2.822 Furuyama, 2006, Arg452 substitution of the erythroid-specific 5-aminolaevulinate synthase, a hot spot mutation in X-linked sideroblastic anaemia, does not itself affect enzyme activity, Eur J Haematol, 76, 33, 10.1111/j.1600-0609.2005.00541.x Furuyama, 2000, Interaction between succinyl CoA synthetase and the heme-biosynthetic enzyme ALAS-E is disrupted in sideroblastic anemia, J Clin Invest, 105, 757, 10.1172/JCI6816 Kaneko, 2009, Hypoxia induces erythroid-specific 5-aminolevulinate synthase expression in human erythroid cells through transforming growth factor-beta signaling, FEBS J, 276, 1370, 10.1111/j.1742-4658.2009.06878.x Guernsey, 2009, Mutations in mitochondrial carrier family gene SLC25A38 cause nonsyndromic autosomal recessive congenital sideroblastic anemia, Nat Genet, 41, 651, 10.1038/ng.359 Ye, 2010, Glutaredoxin 5 deficiency causes sideroblastic anemia by specifically impairing heme biosynthesis and depleting cytosolic iron in human erythroblasts, J Clin Invest, 120, 1749, 10.1172/JCI40372 Allikmets, 1999, Mutation of a putative mitochondrial iron transporter gene (ABC7) in X-linked sideroblastic anemia and ataxia (XLSA/A), Hum Mol Genet, 8, 743, 10.1093/hmg/8.5.743 Bykhovskaya, 2004, Missense mutation in pseudouridine synthase 1 (PUS1) causes mitochondrial myopathy and sideroblastic anemia (MLASA), Am J Hum Genet, 74, 1303, 10.1086/421530 Ricketts, 2006, Thiamine-responsive megaloblastic anaemia syndrome: long-term follow-up and mutation analysis of seven families, Acta Paediatr, 95, 99, 10.1080/08035250500323715 Rotig, 1989, Mitochondrial DNA deletion in Pearson’s marrow/pancreas syndrome, Lancet, 1, 902, 10.1016/S0140-6736(89)92897-3 Bergmann, 2010, Systematic molecular genetic analysis of congenital sideroblastic anemia: evidence for genetic heterogeneity and identification of novel mutations, Pediatr Blood Cancer, 54, 273, 10.1002/pbc.22244 Cotter, 1994, X-linked sideroblastic anemia: identification of the mutation in the erythroid-specific delta-aminolevulinate synthase gene (ALAS2) in the original family described by Cooley, Blood, 84, 3915, 10.1182/blood.V84.11.3915.bloodjournal84113915 Cotter, 1995, Late-onset X-linked sideroblastic anemia. Missense mutations in the erythroid delta-aminolevulinate synthase (ALAS2) gene in two pyridoxine-responsive patients initially diagnosed with acquired refractory anemia and ringed sideroblasts, J Clin Invest, 96, 2090, 10.1172/JCI118258 Prades, 1995, A new mutation of the ALAS2 gene in a large family with X-linked sideroblastic anemia, Hum Genet, 95, 424, 10.1007/BF00208968 Furuyama, 1998, R411C mutation of the ALAS2 gene encodes a pyridoxine-responsive enzyme with low activity, Br J Haematol, 103, 839, 10.1046/j.1365-2141.1998.01050.x Harigae, 1999, A novel mutation of the erythroid-specific delta-Aminolevulinate synthase gene in a patient with non-inherited pyridoxine-responsive sideroblastic anemia, Am J Hematol, 62, 112, 10.1002/(SICI)1096-8652(199910)62:2<112::AID-AJH9>3.0.CO;2-L Furuyama, 2003, Late-onset X-linked sideroblastic anemia following hemodialysis, Blood, 101, 4623, 10.1182/blood-2002-09-2804 Ferreira, 1993, Heme biosynthesis in mammalian systems: evidence of a Schiff base linkage between the pyridoxal 5’-phosphate cofactor and a lysine residue in 5-aminolevulinate synthase, Protein Sci, 2, 1959, 10.1002/pro.5560021117 Gong, 1995, Aminolevulinate synthase: functionally important residues at a glycine loop, a putative pyridoxal phosphate cofactor-binding site, Biochemistry, 34, 1678, 10.1021/bi00005a024 Tan, 1996, Active site of 5-aminolevulinate synthase resides at the subunit interface. Evidence from in vivo heterodimer formation, Biochemistry, 35, 8934, 10.1021/bi952918m Gong, 1998, Aspartate-279 in aminolevulinate synthase affects enzyme catalysis through enhancing the function of the pyridoxal 5’-phosphate cofactor, Biochemistry, 37, 3509, 10.1021/bi9719298 Tan, 1998, The role of tyrosine 121 in cofactor binding of 5-aminolevulinate synthase, Protein Sci, 7, 1208, 10.1002/pro.5560070516 Tan, 1998, Role of arginine 439 in substrate binding of 5-aminolevulinate synthase, Biochemistry, 37, 1478, 10.1021/bi971928f Turbeville, 2007, Histidine 282 in 5-aminolevulinate synthase affects substrate binding and catalysis, Biochemistry, 46, 5972, 10.1021/bi062053k Lendrihas, 2009, Arg-85 and Thr-430 in murine 5-aminolevulinate synthase coordinate acyl-CoA-binding and contribute to substrate specificity, Protein Sci, 18, 1847, 10.1002/pro.195 Lendrihas, 2010, Serine 254 enhances an induced fit mechanism in murine 5-aminolevulinate synthase, J Biol Chem, 285, 3351, 10.1074/jbc.M109.066548 Lendrihas, 2010, Targeting the active site gate to yield hyperactive variants of 5-aminolevulinate synthase, J Biol Chem, 285, 13704, 10.1074/jbc.M109.074237 Zhang, 2002, Transient state kinetic investigation of 5-aminolevulinate synthase reaction mechanism, J Biol Chem, 277, 44660, 10.1074/jbc.M203584200