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Homology between the α and β subunits of chloroplast and bacterial proton‐translocating ATPases
Author(s) -
Deno Hiroshi,
Sugiura Masahiro
Publication year - 1984
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(84)81127-8
Subject(s) - chloroplast , escherichia coli , homology (biology) , atpase , biochemistry , protein subunit , biology , nucleotide , peptide sequence , nucleic acid sequence , amino acid , enzyme , chemistry , gene
The α and β subunits of tobacco chloroplast proton‐translocating ATPase show 25% sequence homology. When these subunits from tobacco chloroplast and Escherichia coli are compared, 66 amino acid residues are identical and the majority of them are localized in 4 regions. Some nucleotide‐binding enzymes contain sequences homologous to the 4 regions, suggesting that these regions have common functions in catalysis.