Nucleotide sequence of the rice cytoplasmic aldolase cDNA
Author(s) -
Soh Hidaka,
Koh-ichi Kadowaki,
Kenichi Tsutsumi,
Kiichi Ishikawa
Publication year - 1990
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/18.13.3991
Subject(s) - biology , complementary dna , nucleic acid sequence , aldolase a , genetics , base sequence , sequence (biology) , peptide sequence , primer (cosmetics) , nucleotide , cytoplasm , microbiology and biotechnology , gene , enzyme , biochemistry , chemistry , organic chemistry
The cDNA coding for a cytoplasmic aldolase (cALD) of rice plant (Oryza sativa L. cv. Nihonbare) was cloned by screening from rice cDNA library with a cDNA probe (pMX71) specific to the maize cALD, kindly supplied by Freeling.M. (1). The sequence of two overlapping cDNA clones contained an open reading frame coding for a protein of 358 amino acids. Of the deduced amino acid sequence, 92% was identical with that of the maize cALD (2) by considering an insertion (residue 342-344) at the C-terminal region (residue 342 of the maize cALD).
Accelerating Research
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom
Address
John Eccles HouseRobert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom