Structural organization of the mouse mitochondrial aspartate aminotransferase gene

Tsuzuki, Teruhisa; Obaru, Kenshi; Setoyama, Chiaki; Shimada, Kazunori

doi:10.1016/0022-2836(87)90454-2

Cited by 49 publications

(40 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…both genes originating either A C A C T C G A G G G G G T G A C A G A G T G C T G G T G C C A~T G A G C C C G T G G G~G A G G T C T T C T T G A G G A G A A A C A T C T T C C C A~C T G C A~C T G G A G T A T C A T G G G G A C C C G The separation of the exon of the presequence from that of the N-terminus of the mature part by a large intron together with the finding of highly repetitive DNA flanking the chicken mAspAT gene and the probable existence of mAspAT pseudogenes in both chicken ( Fig. 1) and mouse [19] (there is no evidence for the existence of pseudogenes of the cytosolic isoenzyme in the two species), as well as the existence of several pseudogenes of mitochondrial malate dehydrogenase, but not of its cytosolic isoenzyme [21,22], suggest that recombination occurs more frequently in the genomic environment of the mAspAT genes than in the environmental of the cAspAT genes. In accord with this hypothesis, some mAspAT clones showed restriction-fragment-length polymorphism in the 3'-end-flanking region, while none of the cAspAT clones did (data not shown).…”

Section: Discussionmentioning

confidence: 96%

“…The part of the mAspAT gene corresponding to the mature part of the protein is 6.0 kb long. The length of the entire gene, as estimated from the genomic Southern blot, is approximately 10 kb, less than half of the approximately 25 kb of the mouse mAspAT gene [19]. The first exon of the sequenced mAspAT clone begins within the codon of Ser3, the first amino acid residue of mature mAspAT (the numbering of amino acid residues corresponds to that in porcine cAspAT [2,4]).…”

Section: Discussionmentioning

confidence: 99%

“…The noncoding upstream region is devoid of a TATA box and is rich in G and C (Fig. 4) and thus probably contains a promoter similar to that found in the genes of mouse AspATs [19,201 and many other house-keeping proteins. The 3'-noncoding end was mapped by aligning the genomic sequence with the sequence of the 3'-noncoding region of the corresponding cDNA.…”

Section: Structure Qf the Noncoding And Flanking Regionsmentioning

confidence: 91%

“…198 Biol. 200,[13][14][15][16][17][18][19][20][21][22]] reveals closely similar structures: in the gene of both the mitochondrial and the cytosolic isoenzyme all but one intron positions are conserved in the two species and five introns out of nine are placed at the same positions in all four genes indicating that the introns were in place before the genes of the two isoenzymes diverged.…”

mentioning

confidence: 99%

“…In addition to their function in the metabolism of amino acids, the AspAT isoenzymes cooperate with the malate dehydrogenase isoenzymes in the malateaspartate shuttle between cytosol and mitochondria [18]. The structural organization of the genes of both AspAT isoenzymes [19,201 and both malate dehydrogenase isoenzymes [21, 221 of the mouse have recently been reported.…”

mentioning

confidence: 99%

See 4 more Smart Citations

Structure of the genes of two homologous intracellularly heterotopic isoenzymes

Juretić

Mattes

Ziak

et al. 1990

European Journal of Biochemistry

View full text Add to dashboard Cite

The genes of mitochondrial and cytosolic aspartate aminotransferase of chicken were cloned and sequenced. In both genes nine exons encode the mature enzyme. The additional exon for the N-terminal presequence that directs mitochondrial aspartate aminotransferase into the mitochondria is separated by the largest intron from the rest of the gene. A comparison of the two genes of chicken with the aspartate aminotransferase genes of mouse [Tsuzuki, T., Obaru, K., Setoyama, C. & Shimada, K. (1987) J . Mol. Biol. 198, 21 -31; Obaru, K., Tsuzuki, T., Setoyama, C. & Shimada, K. (1988) J . Mol. Biol. 200,[13][14][15][16][17][18][19][20][21][22] reveals closely similar structures: in the gene of both the mitochondrial and the cytosolic isoenzyme all but one intron positions are conserved in the two species and five introns out of nine are placed at the same positions in all four genes indicating that the introns were in place before the genes of the two isoenzymes diverged.The variant consensus sequence (T/C),,T(C/T)AG at the 3' splice site of the introns of the genes for nuclearencoded mitochondrial proteins, which had been deduced from a total of 34 introns [Juretik, N., Jaussi, R., Mattes, U. & Christen, P. (1987) Nucleic Acids Res. 15, 10083-100861, was confirmed by including an additional 22 introns into the comparison. The position -4 at the 3' splice site is occupied by base T in 43% of the total 56 introns and appears to be subject to a special evolutionary constraint in this particular group of genes.The following course of evolution of the aspartate aminotransferase genes is proposed. Originating from a common ancestor, the genes of the two isoenzymes intermediarily evolved in separate lineages, i.e. the ancestor eukaryotic and ancestor endosymbiontic cells. When endosymbiosis was established, part of the endosymbiontic genome, including the aspartate aminotransferase gene, was transferred to the nucleus. This process probably led to the conservation of certain splicing factors specific for nuclear-encoded mitochondrial proteins. The presequence for the mitochondrial isoenzyme was acquired by DNA rearrangement. In the eukaryotic lineage, the mitochondrial isoenzyme evolved more slowly than its cytosolic counterpart.Aspartate aminotransferase (AspAT) is the most extensively investigated pyridoxal-5'-phosphate-dependent enzyme functioning in amino acid metabolism (for a review, see [l]). Two distinct isoenzymes of AspAT exist in all higher eukaryotes, one being located in the cytosol (cAspAT) and the other in the mitochondria (mAspAT). The isoenzymes are homologous proteins and are both coded for by nuclear DNA. The complete amino acid sequences of the two isoenzymes from pig [2-41, chicken [5, 61 and horse [7] have been determined. The nucleotide sequences of the cDNAs for both isoenzymes are known for chicken [8, 91, mouse [lo], rat [I 1, 121 and pig [13,14]. Mitochondria1 AspAT is one ofthe typical nuclear-encoded mitochondrial proteins that are synthesized as larger precursors on free ribosomes in the cytoso...

show abstract

Section: Discussionmentioning

confidence: 96%

Section: Discussionmentioning

confidence: 99%

Section: Structure Qf the Noncoding And Flanking Regionsmentioning

confidence: 91%

mentioning

confidence: 99%

mentioning

confidence: 99%

See 3 more Smart Citations

Structure of the genes of two homologous intracellularly heterotopic isoenzymes

Juretić

Mattes

Ziak

et al. 1990

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

The Molecular Evolution of Pyridoxal‐5′‐Phosphate‐Dependent Enzymes

Mehta

Christen

2000

Advances in Enzymology - And Related Areas of Molecular Biology

140

159

View full text Add to dashboard Cite

Transfer of rpl22 to the nucleus greatly preceded its loss from the chloroplast and involved the gain of an intron.

et al. 1991

View full text Add to dashboard Cite

Most chloroplast and mitochondrial proteins are encoded by nuclear genes that once resided in the organellar genomes. Transfer of most of these genes appears to have occurred soon after the endosymbiotic origin of organelles, and so little is known about the process. Our efforts to understand how chloroplast genes are functionally transferred to the nuclear genome have led us to discover the most recent evolutionary gene transfer yet described. The gene rpl22, encoding chloroplast ribosomal protein CL22, is present in the chloroplast genome of all plants examined except legumes, while a functional copy of rpl22 is located in the nucleus of the legume pea. The nuclear rpl22 gene has acquired two additional domains relative to its chloroplast ancestor: an exon encoding a putative N‐terminal transit peptide, followed by an intron which separates this first exon from the evolutionarily conserved, chloroplast‐derived portion of the gene. This gene structure suggests that the transferred region may have acquired its transit peptide by a form of exon shuffling. Surprisingly, phylogenetic analysis shows that rpl22 was transferred to the nucleus in a common ancestor of all flowering plants, at least 100 million years preceding its loss from the legume chloroplast lineage.

show abstract

Structural organization of the mouse mitochondrial aspartate aminotransferase gene

Cited by 49 publications

References 42 publications

Structure of the genes of two homologous intracellularly heterotopic isoenzymes

Structure of the genes of two homologous intracellularly heterotopic isoenzymes

The Molecular Evolution of Pyridoxal‐5′‐Phosphate‐Dependent Enzymes

Transfer of rpl22 to the nucleus greatly preceded its loss from the chloroplast and involved the gain of an intron.

Contact Info

Product

Resources

About