<it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)

<p>Abstract</p> <p>Background</p> <p>Geminiviruses are emerging plant viruses that infect a wide variety of vegetable crops, ornamental plants and cereal crops. They undergo recombination during co-infections by different species of geminiviruses and give rise to more v...

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Main Authors: Mukherjee Sunil K, Choudhury Nirupam R, Pasumarthy Kalyan K
Format: Article
Language:English
Published: BMC 2010-06-01
Series:Virology Journal
Online Access:http://www.virologyj.com/content/7/1/128
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spelling doaj-46a8cba9735843c0aa4b677d42148d5f2020-11-25T02:28:45ZengBMCVirology Journal1743-422X2010-06-017112810.1186/1743-422X-7-128<it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)Mukherjee Sunil KChoudhury Nirupam RPasumarthy Kalyan K<p>Abstract</p> <p>Background</p> <p>Geminiviruses are emerging plant viruses that infect a wide variety of vegetable crops, ornamental plants and cereal crops. They undergo recombination during co-infections by different species of geminiviruses and give rise to more virulent species. Antiviral strategies targeting a broad range of viruses necessitate a detailed understanding of the basic biology of the viruses. ToLCKeV, a virus prevalent in the tomato crop of Kerala state of India and a member of genus Begomovirus has been used as a model system in this study.</p> <p>Results</p> <p>AC3 is a geminiviral protein conserved across all the begomoviral species and is postulated to enhance viral DNA replication. In this work we have successfully expressed and purified the AC3 fusion proteins from <it>E. coli</it>. We demonstrated the higher order oligomerization of AC3 using sucrose gradient ultra-centrifugation and gel-filtration experiments. In addition we also established that ToLCKeV AC3 protein interacted with cognate AC1 protein and enhanced the AC1-mediated ATPase activity in vitro.</p> <p>Conclusions</p> <p>Highly hydrophobic viral protein AC3 can be purified as a fusion protein with either MBP or GST. The purification method of AC3 protein improves scope for the biochemical characterization of the viral protein. The enhancement of AC1-mediated ATPase activity might lead to increased viral DNA replication.</p> http://www.virologyj.com/content/7/1/128
collection DOAJ
language English
format Article
sources DOAJ
author Mukherjee Sunil K
Choudhury Nirupam R
Pasumarthy Kalyan K
spellingShingle Mukherjee Sunil K
Choudhury Nirupam R
Pasumarthy Kalyan K
<it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)
Virology Journal
author_facet Mukherjee Sunil K
Choudhury Nirupam R
Pasumarthy Kalyan K
author_sort Mukherjee Sunil K
title <it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)
title_short <it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)
title_full <it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)
title_fullStr <it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)
title_full_unstemmed <it>Tomato leaf curl Kerala virus </it>(ToLCKeV) AC3 protein forms a higher order oligomer and enhances ATPase activity of replication initiator protein (Rep/AC1)
title_sort <it>tomato leaf curl kerala virus </it>(tolckev) ac3 protein forms a higher order oligomer and enhances atpase activity of replication initiator protein (rep/ac1)
publisher BMC
series Virology Journal
issn 1743-422X
publishDate 2010-06-01
description <p>Abstract</p> <p>Background</p> <p>Geminiviruses are emerging plant viruses that infect a wide variety of vegetable crops, ornamental plants and cereal crops. They undergo recombination during co-infections by different species of geminiviruses and give rise to more virulent species. Antiviral strategies targeting a broad range of viruses necessitate a detailed understanding of the basic biology of the viruses. ToLCKeV, a virus prevalent in the tomato crop of Kerala state of India and a member of genus Begomovirus has been used as a model system in this study.</p> <p>Results</p> <p>AC3 is a geminiviral protein conserved across all the begomoviral species and is postulated to enhance viral DNA replication. In this work we have successfully expressed and purified the AC3 fusion proteins from <it>E. coli</it>. We demonstrated the higher order oligomerization of AC3 using sucrose gradient ultra-centrifugation and gel-filtration experiments. In addition we also established that ToLCKeV AC3 protein interacted with cognate AC1 protein and enhanced the AC1-mediated ATPase activity in vitro.</p> <p>Conclusions</p> <p>Highly hydrophobic viral protein AC3 can be purified as a fusion protein with either MBP or GST. The purification method of AC3 protein improves scope for the biochemical characterization of the viral protein. The enhancement of AC1-mediated ATPase activity might lead to increased viral DNA replication.</p>
url http://www.virologyj.com/content/7/1/128
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