Nucleotide sequence of rat S- decarboxylase cDNA. Comparison with an intronless rat pseudogene

Pulkka, Anitta E.; Keränen, Marja-Riitta; Salmela, Anne; Salmikangas, Paula; Ihalainen, Ritva; Pajunen, Antti

doi:10.1016/0378-1119(90)90279-z

Cited by 19 publications

(14 citation statements)

References 25 publications

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“…On the basis of their sequence homology with two known full-length plant SAMDC sequences of potato [15,33] and spinach [4] we conclude that this ORF represents an SAMDC mRNA of Tritordeum. This conclusion is further supported by the presence of several highly conserved regions documented in all known SAMDC sequences of plants, mammals and yeast [4,14,15,19,22,35] (Fig. 2).…”

Section: Discussionsupporting

confidence: 64%

“…Identical amino acids in at least 3 different sequences are outlined in grey. Amino acids being identical in all 4 sequences listed and in SAMDC sequences of spinach [4], mouse [30,35], rat [22], golden hamster [34] and cow [ 10] are marked by asterisks. The triangle indicates a putative cleavage site of the SAMDC pro-enzyme and the black bar the putative PEST sequence.…”

Section: Isolation and Sequence Analysis Of Cdna Clones 47/11 And 50amentioning

confidence: 99%

“…The similarity between the plant SAMDCs and those of yeast or mammals is much lower, at about 35~o (e.g. [14,22,30]). Figure 2 shows an alignment of the deduced amino acid sequence of the Tritordeum ORF with known SAMDC sequences of potato [33], yeast [ 14] and human [ 19] as an example for mammalian SAMDCs.…”

Section: Tgttgtcgtgcgtcgtttggttactgtgaagcag~cc~ctattgctactctcaandatajl%mentioning

confidence: 99%

“…Despite a striking conservation of amino acid sequences among the mammalian SAMDCs, there is little similarity between the sequences of mammalian, yeast and Escherichia coli enzymes [ 14,20,22,30,34]. Although SAMDC activity could be demonstrated in a variety of plant species [8] only a few fulllength plant sequences have been reported until now (e.g.…”

Section: Introductionmentioning

confidence: 99%

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Isolation and characterization of a Tritordeum cDNA encoding S-adenosylmethionine decarboxylase that is circadian-clock-regulated

Dresselhaus¹,

Barceló

Hagel³

et al. 1996

Plant Mol Biol

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Sequence analysis of the two cDNA clones 47/11 and 50A which were isolated by differential screening of an explant cDNA library obtained from the monocot Tritordeum (hexaploid hybrid of diploid wild barley and tetraploid wheat lines) reveals that both clones include the same open reading frame (ORF). The sequence of this ORF shows a high degree of similarity with dicot S-adenosylmethionine decarboxylase (SAMDC) gene sequences and contains regions highly conserved in all known SAMDC sequences. It is further shown that the sequence represented by the cDNA clones 47/11 and 50A is derived from the wild barley (Hordeum chilense) genome, where it is present as a single-copy gene. Northern analyses indicate the corresponding transcript to accumulate in response to wounding and the transcript level changes with a circadian rhythm, having a beak in the middle of the light period. The periodicity continues in constant light, but is changed in constant darkness.

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Section: Discussionsupporting

confidence: 64%

Section: Isolation and Sequence Analysis Of Cdna Clones 47/11 And 50amentioning

confidence: 99%

Section: Tgttgtcgtgcgtcgtttggttactgtgaagcag~cc~ctattgctactctcaandatajl%mentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Isolation and characterization of a Tritordeum cDNA encoding S-adenosylmethionine decarboxylase that is circadian-clock-regulated

Dresselhaus¹,

Barceló

Hagel³

et al. 1996

Plant Mol Biol

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show abstract

“…6) Proenzyme processing generates two non-identical subunits, termed b and a, which are both indispensable components of the mature enzyme. [6][7][8] The coding region nucleotide sequences of rat, 7,9) hamster, 10) and bovine AdoMetDC cDNA exhibited over 90% homology with the human sequence. 7) The deduced amino acid sequences are also very similar, having only 3-7 amino acid differences.…”

Section: -3)mentioning

confidence: 99%

Identification of the Primary Structure and Post-translational Modification of Rat S-Adenosylmethionine Decarboxylase

Wada

Shirahata

2010

Biological & Pharmaceutical Bulletin

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Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of the potato plant (Solanum tuberosum L.)

Taylor¹,

Arif²,

Kumar³

et al. 1992

Plant Mol Biol

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cDNA clones of two genes (TUB8 and TUB13) which show a 25-30-fold increase in transcript in the stolon tip during the early stages of tuberisation, have been isolated by differential screening. These genes are also expressed in leaves, stems and roots and the expression pattern in these organs changes on tuberisation. Southern analysis shows homologous sequences in the non-tuberising wild type potato species Solanum brevidens and in Lycopersicon esculentum (tomato). Sequence analysis reveals a high degree of similarity between the TUB13 cDNA, and a human S-adenosylmethionine decarboxylase gene. The predicted TUB8 peptide sequence shows several repeats of alanine, glutamate and proline which suggests a structural role for the encoded protein.

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Nucleotide sequence of rat S- decarboxylase cDNA. Comparison with an intronless rat pseudogene

Cited by 19 publications

References 25 publications

Isolation and characterization of a Tritordeum cDNA encoding S-adenosylmethionine decarboxylase that is circadian-clock-regulated

Isolation and characterization of a Tritordeum cDNA encoding S-adenosylmethionine decarboxylase that is circadian-clock-regulated

Identification of the Primary Structure and Post-translational Modification of Rat S-Adenosylmethionine Decarboxylase

Expression and sequence analysis of cDNAs induced during the early stages of tuberisation in different organs of the potato plant (Solanum tuberosum L.)

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