Partial structure of the human H-protein gene

Koyata, H; Hiraga, Kenji

doi:10.1016/0006-291x(91)91001-s

Cited by 3 publications

(2 citation statements)

References 11 publications

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“…We determined the structural organization of GCSH and found that its transcription start site was 168 bp upstream from the translation initiation triplet, using the oligo nucleotide-cap method. Koyata and Hiraga (1991b) previously assigned the transcription initiation site to 168 bp upstream of the initiation triplet, by primer extension analysis, essentially agreeing with our result. Their S1 nuclease protection analysis, however, yielded no specific band.…”

Section: Discussionsupporting

confidence: 93%

“…However, mutations in the Hprotein gene have not been identified, despite reports of a patient who was enzymatically deficient in H-protein (Trauner et al 1981;Hiraga et al 1981). Although the genomic organization of the human H-protein gene (GCSH) has been partially described (Koyata and Hiraga 1991b), complete and accurate information is still missing, especially regarding the sequence information for each exon/ intron boundary that is required for single-exon amplification. Furthermore, the chromosomal localization and the transcription initiation site of the GCSH gene remain unknown.…”

Section: Introductionmentioning

confidence: 99%

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Chromosomal localization, structure, single-nucleotide polymorphisms, and expression of the human H-protein gene of the glycine cleavage system (GCSH), a candidate gene for nonketotic hyperglycinemia

Kure

Kojima²,

Kanno³

et al. 2001

J Hum Genet

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Nonketotic hyperglycinemia (NKH) is an inborn error of metabolism caused by deficiency in the glycine cleavage system (GCS); this system consists of four individual constituents, P-, T-, H-, and L-proteins. Several mutations have been identified in P- and T-protein genes, but not in the H-protein gene (GCSH), despite the presence of case reports of H-protein deficiency. To facilitate the mutational and functional analyses of GCSH, we isolated and characterized a human p1-derived artificial chromosome (PAC) clone encoding GCSH. GCSH spanned 13.5kb and consisted of five exons. Using the PAC clone as a probe, we mapped GCSH to chromosome 16q24 by fluorescence in situ hybridization. The transcription initiation site was determined by the oligonucleotide-cap method, and potential binding sites for several transcriptional factors were found in the 5' upstream region. Direct sequencing analysis revealed five single-nucleotide polymorphisms. The expression profiles of P-, T-, and H-protein mRNAs were studied by dot-blot analysis, using total RNA from various human tissues. GCSH was expressed in all 29 tissues examined, while T-protein mRNA was detected in 27 of the 29 tissues. In contrast, the P-protein gene was expressed in a limited number of tissues, such as liver, kidney, brain, pituitary gland, and thyroid gland, suggesting distinct transcriptional regulation of each GCS constituent.

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Section: Discussionsupporting

confidence: 93%

Section: Introductionmentioning

confidence: 99%

Chromosomal localization, structure, single-nucleotide polymorphisms, and expression of the human H-protein gene of the glycine cleavage system (GCSH), a candidate gene for nonketotic hyperglycinemia

Kure

Kojima²,

Kanno³

et al. 2001

J Hum Genet

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H-protein of glycine decarboxylase is encoded by multigene families in Flaveria pringlei and F. cronquistii (Asteraceae)

Bauwe

1995

Molec. Gen. Genet.

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In Flaveria pringlei and F. cronquistii unlike other plants, H-protein of the glycine cleavage system is encoded by small multigene families. From leaf cDNA libraries and by reverse transcription of mRNA with subsequent polymerase chain reaction (PCR) amplification, we have obtained three different H-protein cDNA clones from each species. The relative levels of total H-protein mRNA, as well as of different H-protein transcripts, have been determined in leaves, stems, and roots of F. pringlei. Stems, with a total of 22% relative to leaves, contain substantial amounts of H-protein transcripts. The corresponding level in roots is relatively low (2.3% relative to leaves) but easily detectable. One of the transcripts occurs only in leaves (HFP20) and another one (HFP13) is present exclusively in photosynthesizing organs. Only one of the H-protein transcripts (HFP4) was found in all three organs, in leaves, stems, and roots of F. pringlei.

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Cloning of the gene (gdcH) encoding H-protein, a component of the glycine decarboxylase complex of pea (Pisum sativum L.)

Macherel

Bourguignon

Douce

1992

Biochemical Journal

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H-protein is the lipoyl-protein component of the glycine decarboxylase complex, which catalyses, with serine hydroxymethyltransferase, the mitochondrial step of photorespiration in plants. We have isolated and characterized the gene (gdcH) encoding the H-protein in pea (Pisum sativum L.). The H-protein gene is distributed in a stretch of about 1.55 kbp and contains three introns (75, 64 and 185 bp) located in the coding region. No intervening sequences were detected in the 5' and 3' non-coding regions. This intron-exon structure contrasts with the preliminary H-protein gene structures reported for human and chicken, where these genes (dispersed on 13 and 8 kbp genomic fragments respectively) are composed of five highly conserved exons and are interrupted by four long introns. Two main transcription sites were detected by primer extension of RNA. The first transcriptional initiation site was assigned the +1 position and correlated with a putative TATA box located at position -26. The second transcriptional start site was not correlated with a putative TATA box, but may be regulated by an 'initiator' element described by Smale & Baltimore [(1989) Cell (Cambridge, Mass.) 57, 103-113] which contains, within itself, the transcription start site. The presence of two potential promoters may be related to the specialized overexpression pattern of H-protein in leaves, in order to support photorespiration.

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Partial structure of the human H-protein gene

Cited by 3 publications

References 11 publications

Chromosomal localization, structure, single-nucleotide polymorphisms, and expression of the human H-protein gene of the glycine cleavage system (GCSH), a candidate gene for nonketotic hyperglycinemia

Chromosomal localization, structure, single-nucleotide polymorphisms, and expression of the human H-protein gene of the glycine cleavage system (GCSH), a candidate gene for nonketotic hyperglycinemia

H-protein of glycine decarboxylase is encoded by multigene families in Flaveria pringlei and F. cronquistii (Asteraceae)

Cloning of the gene (gdcH) encoding H-protein, a component of the glycine decarboxylase complex of pea (Pisum sativum L.)

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