Nucleotide sequence of pea cDNA encoding chloroplast carbonic anhydrase.
Nucleotide sequence of pea cDNA encoding chloroplast carbonic anhydrase.
复制标题
编码叶绿体碳酸酐酶的豌豆 cDNA 的核苷酸序列。
DOI:
10.1093/nar/18.11.3413
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发表时间:
1990
影响因子:
14.9
通讯作者:
W. Ogren
中科院分区:
文献类型:
--
作者:
C. Roeske;W. Ogren
A 1.3 kb cDNA was isolated from a pea (Pisum sativum L.) cDNA library by immunoscreening with rabbit antiserum to spinach carbonic anhydrase (EC 4.2. 1.1). The 984 bp open reading frame contained the entire coding region of the mature chloroplast protein and its transit peptide. The identity of the protein is verified by the strong homology with carbonic anhydrase from spinach (1). There is little sequence homology with mammalian isozymes (2). The transit peptide, based on Edman degradation of the mature polypeptide, is 104 amino acids. This is longer than commonly found for nuclear-encoded chloroplast proteins (3). Also unusual, even for the serine-and theonine-rich chloroplast transit peptides, is a region of seven consecutive Ser residues bounded by Thr residues (amino acid residues 36-43). The molecular mass of the deduced 224 amino acid mature chloroplast polypeptide is 24.2 kd.