Molecular cloning and nucleotide sequence of full-length cDNA for sweet potato catalase mRNA
- PMID: 2885193
- DOI: 10.1111/j.1432-1033.1987.tb11457.x
Molecular cloning and nucleotide sequence of full-length cDNA for sweet potato catalase mRNA
Abstract
A nearly full-length cDNA clone for catalase (pCAS01) was obtained through immunological screening of cDNA expression library constructed from size-fractionated poly(A)-rich RNA of wounded sweet potato tuberous roots by Escherichia coli expression vector-primed cDNA synthesis. Two additional catalase cDNA clones (pCAS10 and pCAS13), which contained cDNA inserts slightly longer than that of pCAS01 at their 5'-termini, were identified by colony hybridization of another cDNA library. Those three catalase cDNAs contained primary structures not identical, but closely related, to one another based on their restriction enzyme and RNase cleavage mapping analyses, suggesting that microheterogeneity exists in catalase mRNAs. The cDNA insert of pCAS13 carried the entire catalase coding capacity, since the RNA transcribed in vitro from the cDNA under the SP6 phage promoter directed the synthesis of a catalase polypeptide in the wheat germ in vitro translation assay. The nucleotide sequencing of these catalase cDNAs indicated that 1900-base catalase mRNA contained a coding region of 1476 bases. The amino acid sequence of sweet potato catalase deduced from the nucleotide sequence was 35 amino acids shorter than rat liver catalase [Furuta, S., Hayashi, H., Hijikata, M., Miyazawa, S., Osumi, T. & Hashimoto, T. (1986) Proc. Natl Acad. Sci. USA 83, 313-317]. Although these two sequences showed only 38% homology, the sequences around the amino acid residues implicated in catalytic function, heme ligand or heme contact had been well conserved during evolution.
Similar articles
-
Primary structure of a precursor for the delta-subunit of sweet potato mitochondrial F1-ATPase deduced from full length cDNA.J Biol Chem. 1990 Apr 15;265(11):6079-85. J Biol Chem. 1990. PMID: 1690722
-
Molecular cloning and expression in Escherichia coli of cDNA encoding the subunit of sweet potato beta-amylase.J Biochem. 1991 Aug;110(2):196-201. doi: 10.1093/oxfordjournals.jbchem.a123556. J Biochem. 1991. PMID: 1837016
-
Complete nucleotide sequence of cDNA and deduced amino acid sequence of rat liver catalase.Proc Natl Acad Sci U S A. 1986 Jan;83(2):313-7. doi: 10.1073/pnas.83.2.313. Proc Natl Acad Sci U S A. 1986. PMID: 3455767 Free PMC article.
-
Characterization of catalase transcripts and their differential expression in maize.Biochim Biophys Acta. 1988 Nov 10;951(1):104-16. doi: 10.1016/0167-4781(88)90030-9. Biochim Biophys Acta. 1988. PMID: 2461221
-
Molecular cloning, cDNA structure, and regulation of the regulatory subunit of type II cAMP-dependent protein kinase from rat ovarian granulosa cells.J Biol Chem. 1986 Sep 15;261(26):12352-61. J Biol Chem. 1986. PMID: 2427518
Cited by
-
Cloning, characterization, and expression in Escherichia coli of a gene encoding Listeria seeligeri catalase, a bacterial enzyme highly homologous to mammalian catalases.J Bacteriol. 1991 Aug;173(16):5159-67. doi: 10.1128/jb.173.16.5159-5167.1991. J Bacteriol. 1991. PMID: 1860824 Free PMC article.
-
Molecular evolutionary analysis based on the amino acid sequence of catalase.J Mol Evol. 1993 Jul;37(1):71-6. doi: 10.1007/BF00170464. J Mol Evol. 1993. PMID: 8360921
-
Isolation and characterization of a pea catalase cDNA.Plant Mol Biol. 1991 Dec;17(6):1263-5. doi: 10.1007/BF00028744. Plant Mol Biol. 1991. PMID: 1932700 No abstract available.
-
Molecular cloning and nucleotide sequence of a cDNA encoding catalase from tomato.Plant Physiol. 1992 Nov;100(3):1605-6. doi: 10.1104/pp.100.3.1605. Plant Physiol. 1992. PMID: 16653169 Free PMC article. No abstract available.
-
Isolation and Abiotic Stress Resistance Analyses of a Catalase Gene from Ipomoea batatas (L.) Lam.Biomed Res Int. 2017;2017:6847532. doi: 10.1155/2017/6847532. Epub 2017 May 30. Biomed Res Int. 2017. PMID: 28638833 Free PMC article.
MeSH terms
Substances
Associated data
- Actions
LinkOut - more resources
Full Text Sources
Other Literature Sources