| Literature DB >> 8918546 |
E Jacquot1, L S Hagen, M Jacquemond, P Yot.
Abstract
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 sequence-nonspecific manner. Moreover, this binding activity was progressively lost as the C-terminus was gradually deleted.Entities:
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Year: 1996 PMID: 8918546 DOI: 10.1006/viro.1996.0587
Source DB: PubMed Journal: Virology ISSN: 0042-6822 Impact factor: 3.616