Nucleic Acids Research, 1995, Vol. 23, No. 6 910-916
© 1995
MOLECULAR BIOLOGY |
Determination of the origin cleavage and joining domain of geminivirus Rep proteins
Max-Planck-Institut für Z
chtungsforschung Carl-von-Linné-Weg 10, D-50829 KÖln, Germany
1Institut des Sciences Végétales CNRS, Avenue de la Terrasse, F-91198 Gif-sur-Yvette, France
*To whom correspondence should be addressed
Received January 13, 1995. Revised February 13, 1995. Accepted February 13, 1995.
Replication of the single-stranded DNA genome of plant geminiviruses follows a rolling circle mechanism, It strictly depends on a ‘rolling circle replication initiator protein’, the Mr 41 kDa viral Rep protein, encoded by the C1 or AC1 genes. Using wheat dwarf virus (WDV) and tomato yellow leaf curl virus (TYLCV) as examples, we show that not only the full-size Rep proteins, but also a putative 30 kDa translation product of WDV open reading frame C1-N as well as an artificially shortened 24 kDa Rep of TYLCV, cleave and join single-stranded origin DNA in vitro. Thus the pivotal origin recognition and processing activities of geminivirus Rep proteins must be mediated by the amino-terminal domain of Rep.
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