Abstract:
:The function of rice dwarf virus segment 11 and the corresponding segments of other phytoreoviruses is not yet determined. The amino acid sequence of Pns11, encoded by segment 11, contains a putative zinc finger and five flanking basic regions at the C-terminus. The full-length Pns11 protein and three truncated derivatives, which lack the N-terminus, the zinc-finger or the C-terminal five basic regions were expressed in Escherichia coli and their nucleic acid binding properties were studied. Pns11 interacts with single- and double-stranded forms of DNA and RNA in a sequence-nonspecific manner. The truncated derivative which contains both the zinc-finger and the C-terminal basic regions has the same binding properties as the full-length Pns11. However, removal of either of these domains prevents binding activity. The binding activity of Pns11 was drastically reduced when the blots were treated with a high concentration of EDTA. Moreover, Pns11 extracted from infected rice also binds to single-stranded RNA. These data suggest that RDV Pns11 binding activity is structure-dependent and it may play an important role in virus replication and/or genome assortment.
journal_name
Virologyjournal_title
Virologyauthors
Xu H,Li Y,Mao Z,Li Y,Wu Z,Qu L,An C,Ming X,Schiemann J,Casper R,Chen Zdoi
10.1006/viro.1997.8945subject
Has Abstractpub_date
1998-01-20 00:00:00pages
267-72issue
2eissn
0042-6822issn
1096-0341pii
S0042-6822(97)98945-5journal_volume
240pub_type
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