The function of the open reading frame 2 product (p2) of cacao swollen shoot virus (CSSV) and of other badnaviruses is not yet determined. Their carboxyl-termini are lysine and proline rich and also contain alanine residues, amino acids present at the C-termini of histone-like proteins. Full-length CSSV p2 (132 amino acids) or versions truncated at the C-terminus (128, 113, 103, or 101 amino acids) were expressed in Escherichia coli and partially purified. When assayed in nucleic acid-binding tests, p2 was able to interact with CSSV and other double-stranded DNAs and with CSSV and other single-stranded RNA transcripts in a sequence-nonspecific manner. Moreover, this binding activity was progressively lost as the C-terminus was gradually deleted. (C) 1996 Academic Press, Inc.
机构:
UNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USAUNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USA
CHEN, L
FRANKEL, AD
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UNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USAUNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USA
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UNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USAUNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USA
CHEN, L
FRANKEL, AD
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UNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USAUNIV CALIF SAN FRANCISCO, GLADSTONE INST VIROL & IMMUNOL, SAN FRANCISCO, CA 94141 USA