Skip Navigation

This Article
Right arrow Full Text Freely available
Right arrow Print PDF (275K) Freely available
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in ISI Web of Science
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Add to My Personal Archive
Right arrow Download to citation manager
Right arrow Search for citing articles in:
ISI Web of Science (30)
Right arrowRequest Permissions
Right arrow Commercial Re-use Guidelines
for Open Access NAR Content
Google Scholar
Right arrow Articles by Cerritelli, S. M.
Right arrow Articles by Crouch, R. J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Cerritelli, S. M.
Right arrow Articles by Crouch, R. J.
Social Bookmarking
Add to CiteULike   Add to Connotea   Add to Del.icio.us  
What's this?

Nucleic Acids Research, Vol 26, Issue 7 1834-1840, Copyright © 1998 by Oxford University Press

ARTICLES

A common 40 amino acid motif in eukaryotic RNases H1 and caulimovirus ORF VI proteins binds to duplex RNAs

SM Cerritelli, OY Fedoroff, BR Reid and RJ Crouch
Laboratory of Molecular Genetics, National Institute of Child Health and Human Development, National Institutes of Health, Bethesda, MD 20892, USA.

Eukaryotic RNases H from Saccharomyces cerevisiae , Schizosaccharomyces pombe and Crithidia fasciculata , unlike the related Escherichia coli RNase HI, contain a non-RNase H domain with a common motif. Previously we showed that S.cerevisiae RNase H1 binds to duplex RNAs (either RNA- DNA hybrids or double-stranded RNA) through a region related to the double-stranded RNA binding motif. A very similar amino acid sequence is present in caulimovirus ORF VI proteins. The hallmark of the RNase H/caulimovirus nucleic acid binding motif is a stretch of 40 amino acids with 11 highly conserved residues, seven of which are aromatic. Point mutations, insertions and deletions indicated that integrity of the motif is important for binding. However, additional amino acids are required because a minimal peptide containing the motif was disordered in solution and failed to bind to duplex RNAs, whereas a longer protein bound well. Schizosaccharomyces pombe RNase H1 also bound to duplex RNAs, as did proteins in which the S.cerevisiae RNase H1 binding motif was replaced by either the C.fasciculata or by the cauliflower mosaic virus ORF VI sequence. The similarity between the RNase H and the caulimovirus domain suggest a common interaction with duplex RNAs of these two different groups of proteins.
Add to CiteULike CiteULike   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us    What's this?


This article has been cited by other articles:


Home page
 Plant Physiol.Home page
P. A. Harries, K. Palanichelvam, W. Yu, J. E. Schoelz, and R. S. Nelson
The Cauliflower Mosaic Virus Protein P6 Forms Motile Inclusions That Traffic along Actin Microfilaments and Stabilize Microtubules
Plant Physiology, February 1, 2009; 149(2): 1005 - 1016.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
P. V. Shivaprasad, R. Rajeswaran, T. Blevins, J. Schoelz, F. Meins Jr, T. Hohn, and M. M. Pooggin
The CaMV transactivator/viroplasmin interferes with RDR6-dependent trans-acting and secondary siRNA pathways in Arabidopsis
Nucleic Acids Res., October 1, 2008; 36(18): 5896 - 5909.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
S. A. Gaidamakov, I. I. Gorshkova, P. Schuck, P. J. Steinbach, H. Yamada, R. J. Crouch, and S. M. Cerritelli
Eukaryotic RNases H1 act processively by interactions through the duplex RNA-binding domain
Nucleic Acids Res., April 14, 2005; 33(7): 2166 - 2175.
[Abstract] [Full Text] [PDF]

Home page
 Plant CellHome page
M. Haas, A. Geldreich, M. Bureau, L. Dupuis, V. Leh, G. Vetter, K. Kobayashi, T. Hohn, L. Ryabova, P. Yot, et al.
The Open Reading Frame VI Product of Cauliflower mosaic virus Is a Nucleocytoplasmic Protein: Its N Terminus Mediates Its Nuclear Export and Formation of Electron-Dense Viroplasms
PLANT CELL, March 1, 2005; 17(3): 927 - 943.
[Abstract] [Full Text] [PDF]

Home page
 J. Gen. Virol.Home page
M. Bureau, V. Leh, M. Haas, A. Geldreich, L. Ryabova, P. Yot, and M. Keller
P6 protein of Cauliflower mosaic virus, a translation reinitiator, interacts with ribosomal protein L13 from Arabidopsis thaliana
J. Gen. Virol., December 1, 2004; 85(12): 3765 - 3775.
[Abstract] [Full Text] [PDF]

Home page
 J. Virol.Home page
K. Kobayashi and T. Hohn
Dissection of Cauliflower Mosaic Virus Transactivator/Viroplasmin Reveals Distinct Essential Functions in Basic Virus Replication
J. Virol., August 1, 2003; 77(15): 8577 - 8583.
[Abstract] [Full Text] [PDF]

Home page
 GeneticsHome page
T. Langdon, G. Jenkins, R. Hasterok, R. N. Jones, and I. P. King
A High-Copy-Number CACTA Family Transposon in Temperate Grasses and Cereals
Genetics, March 1, 2003; 163(3): 1097 - 1108.
[Abstract] [Full Text] [PDF]

Home page
 Nucleic Acids ResHome page
M. L. Engel, J. C. Hines, and D. S. Ray
The Crithidia fasciculata RNH1 gene encodes both nuclear and mitochondrial isoforms of RNase H
Nucleic Acids Res., February 1, 2001; 29(3): 725 - 731.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
H. Wu, W. F. Lima, and S. T. Crooke
Properties of Cloned and Expressed Human RNase H1
J. Biol. Chem., October 1, 1999; 274(40): 28270 - 28278.
[Abstract] [Full Text] [PDF]


Disclaimer: Please note that abstracts for content published before 1996 were created through digital scanning and may therefore not exactly replicate the text of the original print issues. All efforts have been made to ensure accuracy, but the Publisher will not be held responsible for any remaining inaccuracies. If you require any further clarification, please contact our Customer Services Department.