Jacquot E, Hagen L S, Jacquemond M, Yot P
Institut de Biologie Moléculaire des Plantes, Centre National de la Recherche Scientifique, Université Louis Pasteur, Strasbourg, France.
Virology. 1996 Nov 1;225(1):191-5. doi: 10.1006/viro.1996.0587.
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.
可可肿枝病毒(CSSV)开放阅读框2产物(p2)以及其他花椰菜花叶病毒科病毒的功能尚未确定。它们的羧基末端富含赖氨酸和脯氨酸,还含有丙氨酸残基,这些氨基酸存在于类组蛋白的C末端。全长CSSV p2(132个氨基酸)或在C末端截短的变体(128、113、103或101个氨基酸)在大肠杆菌中表达并进行了部分纯化。在核酸结合试验中检测时,p2能够以序列非特异性方式与CSSV及其他双链DNA以及CSSV和其他单链RNA转录本相互作用。此外,随着C末端逐渐缺失,这种结合活性逐渐丧失。