Structure of the rat renin gene

Fukamizu, Akiyoshi; Nishi, Kazuto; Cho, Takeshi; Saitoh, Michiya; Nakayama, Kazuhisa; Ohkubo, Hiroaki; Nakanishi, Shigetada; Murakami, Kazuo

doi:10.1016/0022-2836(88)90151-9

Cited by 83 publications

(44 citation statements)

References 15 publications

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“…Alignment of the barley grain aspartic proteinase with other aspartic proteinases. Alignment of the amino acid sequence of the barleygrain aspartic proteinase (BAP) with the amino acid sequences of porcine cathepsin D (PCD) [45,46], human cathepsin D (HCD) [47], human caihepsin E (HCE) [40], yeast proteinase A (YPA) [3], japanese macaque pepsinogen A (MPA) [48,491, rat renin (RR) [50], calf chymosin (BC) [37], rhizopuspepsin (RP) [51] and yeas; BAR1 (YBI) [41]. The sequences are shown in descending order; the higher a sequence is located the more identical it is with the barley enzyme.…”

Section: Discussionmentioning

confidence: 99%

Primary structure of a barley‐grain aspartic proteinase

Runeberg-Roos

Törmäkangas

Östman

1991

European Journal of Biochemistry

127

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Two enzymatically active heterodimeric forms of an aspartic proteinase, a putative 32 kDa + 16 kDa precursor form and a putative 29 kDa + 11 kDa mature form, are present in resting barley grains (Sarkkinen, P., Kalkkinen, N., Tilgmann, C., Siuro, J., Kervinen, J. & Mikola, L., 1990, in the press). The cDNA corresponding to this enzyme has been cloned and sequenced. The full-length 1863-bp cDNA sequence codes for an open reading frame of 508 amino acids. The open reading frame consists of a 66-amino acid preprosequence and a 442-amino acid mature protein.Comparison of the N-terminal amino acid sequences of the enzyme subunits with the sequence of the cDNA clone indicates that the heterodimeric enzyme is translated as a proenzyme which is processed into two subunits. The localisation of the experimentally determined N-terminal amino acid sequences of all four subunits (32 kDa + 16 kDa and 29 kDa + 11 kDa) in the same transcript, as well as the detection of only one 2.0-kb mRNA on Northern blots from resting seeds, clearly indicates that the larger (32 kDa + 16 kDa) enzyme is an intermediate precursor form of the smaller (29 kDa + 11 kDa) enzyme. The processing pattern of the barley enzyme, which is the first sequenced plant aspartic proteinase, differs from that of all other known aspartic proteinases. The barley enzyme is highly similar to mammalian and yeast aspartic proteinases, especially to human and porcine cathepsin D. This similarity is clearly dispersed over two regions, separated by a dissimilar, barley-specific region of 104 amino acids.In animals and yeast, members of the family of aspartic proteinases, including cathepsin D, renin, chymosin and proteinase A, are very substrate-specific enzymes with well-defined physiological functions. This class of proteinases is involved in the activation of other enzymes, e.g. the lysosomal acid phosphatase and carboxypeptidase Y [l -31 as well as extracellular proteins like procollagen and the prohormonal angiotensinogen [4, 51. Aspartic proteinases are also involved in the digestion and inactivation of specific proteins like the protcinase-inhibitor cystatin and the IC chain of the milk Kcasein [6, 71. A common feature of aspartic proteinases is an active cleft where two aspartate residues play a central role in the catalytic mechanism [S, 91. The amino acid sequences around these aspartate residues are generally conserved. The Note. The novel nucleotide acid sequence data published here has been dcposited with the EMBL sequence data bank and i s available under accession number X56136.Dediwtion. To the memory of Juhani Mikola who initiated this work as a continuation of his research on storage proteins and their mobilisation during germination. activity of most aspartic proteinases is inhibited by the specific inhibitor pepstatin. Different aspartic proteinases differ in their cellular localisation and processing pattern, as well as in their substrate specificity.In plants, aspartic proteinase activity has been localised in seeds from a broad variety of plant sp...

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Section: Discussionmentioning

confidence: 99%

Primary structure of a barley‐grain aspartic proteinase

Runeberg-Roos

Törmäkangas

Östman

1991

European Journal of Biochemistry

127

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“…PCR-directed site-specific mutagenesis of the 2 translation start codons ATG I and ATG II (at position ϩ33 bp and ϩ48 bp with respect to the transcription start site 18 was performed by the use of a 4 primer system with a pair of overlapping internal primers. The total length of the sequence remained unchanged.…”

Section: Site-directed Mutagenesis Of the 2 Translation Start Codonsmentioning

confidence: 99%

“…Previously, 18 1.2 kb of the rat renin promoter region had been cloned. For the present study, a longer 5Ј-flanking region was considered to be necessary to include as many regulatory elements of the promoter region as possible.…”

Section: Cloning Of the Rat Renin Genementioning

confidence: 99%

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Transcriptional Regulation of the Rat Renin Gene by Regulatory Elements in Intron I

Voigtländer

Ganten²,

Bäder³

1999

Hypertension

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Abstract-Renin catalyzes the rate-limiting step in the enzymatic cascade leading to the vasoactive peptide angiotensin II.Therefore, the activity of the renin-angiotensin system in a tissue is regulated significantly at the level of transcription of the renin gene. Besides transcription factor binding sites in the promoter region, the renin genes of human and rat contain regulatory elements also in intron I. Inclusion of intron I in reporter gene constructs with the renin promoter leads to a marked down-regulation of gene expression in nonrenin expressing 293 human embryonic kidney cells but has hardly any effect in renin-expressing L8 rat skeletal myoblasts. In combination with the cytomegalovirus immediate early gene promoter, the silencing occurs in both cell lines but is less pronounced in L8 cells. By partially deleting intron I in these constructs, we describe 5 negative (I-NRE) and 2 positive (I-PRE) regulatory elements responsible for these effects. Using gel-retardation and methylation-interference assays with 293-nuclear extracts, we detected a pseudopalindromic protein-binding sequence between position ϩ159 and ϩ171 relative to the transcriptional start site.

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“…To link the renin promoter obtained from Sprague Dawley rats [1] and the chloramphenicol acetyltransferase (CAT) gene, a 264-bp rat renin DNA molecule containing the putative transcription start site (-238 to + 26) was subcloned into BgIII/HindIII sites of pUCSV0cat [31. A 1.9 kb portion of the linear DNA fragment, rRN023cat, was prepared by digestion with BgIII and Barn HI enzymes from the CAT fusion plasmid and separated by agarose electrophoresis and extracted (Fig.…”

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confidence: 99%