Open AccessThe C‐terminal domain of plant catalases Implications for a glyoxysomal targeting sequence
Author(s) -
GONZÁLEZ Elma
Publication year - 1991
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1991.tb16111.x
Subject(s) - peroxisomal targeting signal , glyoxysome , peroxisome , complementary dna , biochemistry , biology , peptide sequence , amino acid , catalase , enzyme , gene
A castor bean ( Ricinus communis cv. Hale) cDNA encoding catalase was cloned and sequenced. The cDNA encoding the carboxy‐terminal domain of catalase was compared to the corresponding sequences of six other plant catalases. The deduced amino acid sequences were compared according to the chemical attributes of each amino acid within each carboxy‐terminal domain. A tripeptide sequence having the chemical attributes of the peroxisomal targeting sequence [Gould, S. J., Keller, G.‐A., Hosken, N., Wilkinson, J. & Subramani, S. (1989) J. Cell Biol. 108 , 1657–1664] was common to all the glyoxysomal/peroxisomal plant catalases. This sequence motif was located six amino acids from the carboxy terminus of each of the plant catalases. An identical motif was also found within the carboxy‐terminal domain of three mammalian catalases previously sequenced. We hypothesize that these motifs are at least part of the targeting mechanism for catalase entry into plant glyoxysomes/peroxisomes.