A newly discovered human α-globin gene
Tóm tắt
A previously undefined transcript with significant homology to the pseudo-α2 region of the α-globin locus on human chromosome 16 was detected as part of an effort to better define the transcriptional profiles of human reticulocytes. Cloning and sequencing of that transcript (GenBank AY698022; named μ-globin) revealed an insert with a 423-nucleotide open reading frame. BLASTP and ClustalW and phylogenetic analyses of the predicted protein demonstrated a high level of homology with the avian α-D globin. In addition, the heme- and globin-binding amino acids of μ-globin and avian α-D globin are largely conserved. Using quantitative real-time polymerase chain reaction (PCR), μ-globin was detected at a level of approximately 0.1% that measured for α-globin in erythroid tissues. Erythroid-specific expression was detected by Northern blot analysis, and maximal expression during the erythroblast terminal differentiation was also detected. Despite this highly regulated pattern of μ-globin gene transcription, μ-globin protein was not detected by mass spectrometry. These results suggest the human genome encodes a previously unrecognized globin member of the avian α-D family that is transcribed in a highly regulated pattern in erythroid cells. (Blood. 2005;106:1466-1472)
Tài liệu tham khảo
Higgs DR. Vickers MA, Wilkie AO, Pretorius IM, Jarman AP, Weatherall DJ. A review of the molecular genetics of the human alpha globin gene cluster. Blood.1989;73: 1081-1104.
Hsu SL, Marks J, Shaw JP, et al. Structure and expression of the human θ1 globin gene. Nature.1988;331: 94-96.
Marks J, Shaw J-P, Shen C-KJ. Sequence organization and genomic complexity of primate theta1 globin gene, a novel alpha-globin-like gene. Nature.1986;321: 785-788.
Clegg JB. Can the product of the θ gene be a real globin? Nature.1987;329: 465-466.
Albitar M, Care A, Peschle C, Liebhaber SA. Developmental switching of messenger RNA expression from the human alpha globin cluster: fetal/adult pattern of theta-globin gene expression. Blood.1992;80: 1586-1591.
Proudfoot NJ, Gil A, Maniatis T. The structure of the human zeta-globin gene and a closely linked, nearly identical pseudogene. Cell.1982;31: 553-563.
Hardison RC, Sawada I, Cheng J-F, Shen C-K, Schmid CW. A previously undetected pseudogene in the human alpha globin gene cluster. Nucleic Acids Res.1986;14: 1903-1911.
Proudfoot NJ, Maniatis T. The structure of a human alpha globin pseudogene and its relationship to alpha globin gene duplication. Cell.1980;21: 537-544.
The Genome International Sequencing Consortium. Initial sequencing and analysis of the human genome. Nature.2001;409: 860-921.
Baross A, Butterfield YS, Coughlin SM, et al. Systematic recovery and analysis of full-ORF human cDNA clones. Genome Res.2004;14: 2083-2092.
Boguski MS, Lowe TM, Tolstoshev CM. DbEST-database for “expressed sequence tags.” Nat Genet.1993;4: 332-333.
Trinklein ND, Aldred SF, Hartman SJ, Schroeder DI, Otillar RP, Myers RM. An abundance of bidirectional promoters in the human genome. Genome Res.2004;14: 62-66.
Wojda U, Noel P, Miller JL. Fetal and adult hemoglobin production during adult erythropoiesis: coordinate expression correlates with cell proliferation. Blood.2002;99: 3005-3013.
Merchant M, Weinberger SR. Recent advancements in surface-enhanced laser desorption/ionization-time of flight-mass spectrometry. Electrophoresis.2000;21: 1164-1177.
Caputo E, Moharram R, Martin BM. Methods for on-chip protein analysis. Anal Biochem.2003;321: 116-124.
Altschul SF, Gish W, Miller W, Myers EW, Lipman DJ. Basic local alignment search tool. J Mol Biol.1990;215: 403-410.
Kent WJ. BLAT—the BLAST-like alignment tool. Genome Res.2002;12: 656-664.
Scherf M, Klingenhoff A, Werner T. Highly specific localization of promoter regions in large genomic sequences by PromoterInspector: a novel context analysis approach. J Mol Biol.2000;297: 599-606.
Chenna R, Sugawara H, Koike T, Lopez, et al. Multiple sequence alignment with the Clustal series of programs. Nucleic Acids Res.2003;31: 3497-3500.
Rogers JS, Swofford DL. Multiple local maxima for likelihoods of phylogenetic trees: a simulation study. Mol Biol Evol.1999;16: 1079-1085.
Choi JH, Jung HY, Kim HS, Cho HG. PhyloDraw: a phylogenetic tree drawing system. Bioinformatics.2000;16: 1056-1058.
Steinberg MH, Forget BG, Higgs DR, Nagel RL, eds. Disorders of Hemoglobin: Genetics, Pathophysiology, and Clinical Management. Cambridge, United Kingdom: Cambridge University Press; 2001: 201-202.
Kroeger KS, Kundrot CE. Structures of a hemoglobin-based blood substitute: insights into the function of allosteric proteins. Structure.1997;5: 227-237.
Kozak M. An analysis of 5'-noncoding sequences from 699 messenger RNAs. Nucleic Acids Res.1987;15: 8125-8148.
Waggoner SA, Liebhaber SA. Regulation of alpha globin mRNA stability. Exp Biol Med.2003;228: 387-395.
Gorr TA, Cahn JD, Yamagata H, Bunn HF. Hypoxia-induced synthesis of hemoglobin in the crustacean Daphnia magna is hypoxia-inducible factor-dependent. J Biol Chem.2004;279: 36038-36047.
Fung ET, Thulasiraman V, Weinberger SR, Dalmasso EA. Protein biochips for differential profiling. Curr Opin Biotechnol.2001;12: 65-69.
Boissel JP, Kasper TJ, Bunn HF. Cotranslational amino-terminal processing of cytosolic proteins: cell-free expression of site-directed mutants of human hemoglobin. J Biol Chem.1988;263: 8443-8449.
Grimwood J, Gordon LA, Olsen A, et al. The DNA sequence and biology of human chromosome. 19 Nature.2004;428: 529-535.
Proudfoot NJ, Shander MH, Manley JL, Gefter ML, Maniatis T. Structure and in vitro transcription of human globin genes. Science.1980;209: 1329-1336.
Brown JL, Ingram V. Structural studies on chick embryonic hemoglobins. J Biol Chem.1974;249: 3960-3972.
Chapman BS, Hood LE, Tobin AJ. Minor early embryonic chick hemoglobin M. J Biol Chem.1982;257: 651-659.
Hiebl I, Schneeganss D, Braunitzer G. High-altitude respiration of birds: the primary structures of the alpha D-chains of the Bar-headed goose (Anser indicus), the Greylag goose (Anser anser) and the Canada goose (Branta canadensis). Biol Chem Hoppe-Seyler.1986;367: 591-599.
Hiebl I, Schneeganss D, Grimm F, Kösters J, Braunitzer G. The primary structure of the major and minor hemoglobin component of adult European black vulture (Aegypius monachus, Aegypiinae). Biol Chem Hoppe-Seyler.1987;368: 11-18.
Rücknagel KP, Braunitzer G. The primary structure of the major and minor hemoglobin component of adult western painted turtle (Chrysemys picta bellii). Biol Chem Hoppe-Seyler.1988;369: 123-131.
Petruzzelli R, Aureli G, Lania A, Galtieri A, Desideri A, Giardina B. Diving behavior and haemoglobin function: the primary structure of the alpha- and beta-chains of the sea turtle (Caretta caretta) and its functional implications. Biochem J.1996;316: 959-965.
Fushitani K, Higashiyama K, Moriyama EN, Imai K, Hosokawa K. The amino acid sequences of two alpha chains of hemoglobins from Komodo dragon Mu-anus komodoensis and phylogenetic relationships of amniotes. Mol Biol Evol.1996;13: 1039-1043.
Stoeckelhuber M, Gorr T, Kleinschmidt T. The primary structure of three hemoglobin chains from the Indigo snake (Drymachon corais erebennus, Serpentes): first evidence for alpha-D chains and two beta chain types in snakes. Biol Chem.2002;383: 1907-1916.
Bunn HF. Evolution of mammalian hemoglobin function. Blood.1981;58: 189-197.
Southan C. Has the yo-yo stopped? An assessment of human protein-coding gene number. Proteomics.2004;4: 1712-1726.
Snyder M, Gerstein M. Genomics: defining genes in the genomics era. Science.2003;300: 258-260.
Fei YJ, Fujita S, Huisman TH. Two different theta globin gene deletions observed among black newborn babies. Br J Haematol.1988;68: 249-253.
Weatherall DJ, Clegg JB. The Thalassemia Syndromes. 4th ed. Oxford, United Kingdom: Blackwell Scientific; 2001: 133-191.
Perutz MF, Wilkinson AJ, Paoli M, Dodson GG. The stereochemical mechanism of the cooperative effects in hemoglobin revisited. Annu Rev Biophys Biomol Struct.1989;27: 1-34.
Gascuel O. BIONJ: an improved version of the NJ algorithm based on a simple model of sequence data. Mol Biol Evol.1997;14: 685-695.