The complete nucleotide sequence of cDNA encoding phosphoenolpyruvate carboxylase (PEPCase) from cultured tobacco (a C3 plant) cells was determined and the deduced amino acid sequence was compared with those of PEPCases from other higher plants.
cDNA sequence and expression of a phosphoenolpyruvate carboxylase gene from soybean
โ Scribed by Toshio Sugimoto; Tsutomu Kawasaki; Tomohiko Kato; Robert F. Whittier; Daisuke Shibata; Yukio Kawamura
- Publisher
- Springer
- Year
- 1992
- Tongue
- English
- Weight
- 398 KB
- Volume
- 20
- Category
- Article
- ISSN
- 0167-4412
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โฆ Synopsis
A full-length cDNA encoding a subunit of phosphoenolpyruvate carboxylase (PEPC) was isolated from a developing seed expression library of the C3 plant Glycine max. The corresponding mRNA is present at similar levels in leaf, stem, root and developing seed. Two potential start codons exist, and the activity of protein initiated from the first such codon could be subject to regulation by protein kinase. Sequence comparison shows a similar upstream start codon in the case of the Ppc2 gene from Mesembryanthemum crystallinum, previously assumed to lack the sequences necessary for phosphorylation. The soybean encoded protein tends to resemble other 'C3-type' PEPC proteins more closely than those implicated in C4 or crassulacean acid metabolism.
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A gene (SCPEPCD1) encoding phosphoenolpyruvate carboxylase (PEPC) was isolated from the C-4 monocot sugarcane (Saccharum hybrid var. H32-8560). SCPEPCD1 is ca. 6800 bp long, with 10 exons. The entire gene sequence from -1561 to 262 bp downstream of the putative poly(A) addition signal is reported. A
Three different cDNAs for phosphoenolpyruvate carboxylase (PEPC) were isolated from soybean root nodules. The full-length cDNA of the most abundant isoform (GmPEPC7) was very similar to another one (GmPEPC15), the nucleotide sequence of which is identical to that of a reported clone (gmppc1) (Vazque
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