Sequence of human 5-amlnoievulinate synthase cDNA

5-Aminolevulinic acid synthesis in Escherichia coli

“…When it was added to a mixture of tRNAGIU and extract, the effect was very weak. DISCUSSION An E. coli gene which complements the hemA mutation in HU227 encodes a protein, the amino acid sequence of which (Li et al, submitted) shows no homologies with any reported ALA S sequences (human [2], mouse [34], chicken liver [6], Saccharomyces cerevisiae [38], or Bradyrhizobium japonicum [24]), although all of these sequences have certain regions of significant homology. Three ALA-requiring mutants of E. coli have been reported; two, the parent of HU227, SASX41B, and the parent of TB1(pUI553), SHSP19, contain mutations which were mapped at 27 min on the genome, both of which were complemented by pJL68 (32; Li et al, submitted); the other, popC, was mapped at 4 min (29,46 Crude sonicates of JL1268 make appreciable quantities of ALA.…”

Analysis of the polyadenylation consensus sequence context in the genes of nuclear encoded mitochondrial proteins

“…Nucleotide sequence information of Y-ends of all known genes of nuclear-encoded mitochondrial proteins has been used for the analysis: rat cytochrome c [11], (R cyt c); bovine cytochrome P-450 (SSC) [12], (B cytP450); bovine adrenodoxin [13], (B Adrdox); rat ornithine aminotransferase [14], (R OAT); porcine mitochondrial a:~partate aminotransferase [15], (P mAspAT); bovine mitochondrial ATP synthase proteolipid [16], (B P1ATPas, B P2ATPas); human aldehyde dehydrogenase 2 [17], (H ALDH2); rat carbamyl synthetase 1 [18], (R cps); human F1-ATPase (subunit) [19], (H ATPsyn); human cytochrome P-450 (SSC) [20], (H cytP450); chicken 5-aminolevulinate synthase [21], (C 5'ala); bovine ADP/ATP carrier [22], (B ADPATPc); human ornithine aminotransferase [23], (H OAT); mouse asparta~e aminotransferase [24], (M rnAspAT); rat serine; pyruvate aminotransferase [25], (R srpyatase); bovine ATP synthase; precursors for oligomycin sensitivity conferring protein, factor 6 and adenosine° triphosphatase inhibitor protein [26], (B OSCP, B F6, B ATPasin); rat aspartate aminotransferase [27], (R mAspAT); human medium-chain acyl-CoA dehydrogenase [28], (H acylCod); human 5-aminolevulinate synthase [29], (H 5'ala); human subunit 4 of cytochrome oxidase [30], (H coxlV); human ADP/ATP carrier [31], (H ADPATPc); rat EIcz subunit of branched chain ~z-ketoacid dehydrogenase [32], (R E~ BCKD); porcine and human lipoamide dehydrogenase [33], (H LPdehyd, P LPdehyd); bovine adrenodoxin reductase [34], (B Adrdred); bovine steroid l lfl-hydroxylase (p450 ell) [35]. (B cyt45011); rat ornithine carbamoyltransferase [36], (R oct); human pyruvate dehydrogenase EI~ subunit [37], (H PyrDhE1); bovine mitochondrial adenylate kinase 2 [38], (B AK2A, B AK2B); bovine mitochondrial carrier protein [39], (B mtPcP); rat mitochondrial 3-oxoacyl-CoA thiolase [40], (R 3oxCoth); human liver glutamate dehydrogenase [41], (H GDH); rat heart and liver subunit Via of cytochrome oxidase …”

Human erythroid 5-aminolevulinate synthase: promoter analysis and identification of an iron-responsive element in the mRNA.

“…We have previously isolated cDNA clones for the housekeeping ALAS of chick embryo (Borthwick et al, 1985), rat (Srivastava et al, 1988) and human (Bawden et al, 1987) and determined the structure of the chicken housekeeping ALAS gene (Maguire et al, 1986). As a first step towards understanding the molecular regulation of ALAS during erythropoiesis, we report here the characterization of cDNA clones and the gene promoter for human erythroid ALAS.…”