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RNA‐binding protein‐related sequence in a malaria antigen, clustered‐asparagine‐rich protein
Author(s) -
Kuma Keiichi,
Iwabe Naoyuki,
Kawanishi Yuichi,
Miyata Takashi
Publication year - 1990
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(90)80067-s
Subject(s) - asparagine , rna , biology , rna binding protein , peptide sequence , amino acid , sequence alignment , conserved sequence , genetics , microbiology and biotechnology , biochemistry , gene
Members of the RNA‐binding protein superfamily contain RNA binding domains of about 90 amino acids with a highly conserved motif ‘GFGF’. Using the conserved motif with some variations G‐(F/Y)‐(G/A)‐(F/Y)‐(V/I)‐X‐(F/Y) as a probe, we screened protein sequences carrying identical amino acids in an NBRF‐protein database. It has been found that the C‐terminal portion of clustered asparagine‐rich protein (CARP), a malaria antigen from Plasmodium falciparum , shows an unexpected sequence similarity with the RNA‐binding protein superfamily for the C‐terminal half of the RNA‐binding domain. Dot matrix comparisons and alignment of these sequences as well as a statistical test have revealed highly significant sequence similarities. From these analyses, we conclude that the malaria antigen CARP belongs to a large family of the RNA‐binding proteins. An evolutionary implication of the sequence similarity was also discussed.