A Novel Arabidopsis Acetyltransferase Interacts with the Geminivirus Movement Protein NSP

Overview

Journal Plant Cell

Publisher Oxford University Press

Specialties Biology
Cell Biology

Date 2003 Jul 3

PMID 12837950

Citations 31

Authors

Roisin C McGarry

Yoshimi D Barron

Miguel F Carvalho

Janet E Hill

Daniel Gold

Edwin Cheung

W Lee Kraus

Sondra G Lazarowitz

Affiliations

Soon will be listed here.

Abstract

Protein acetylation is important in regulating DNA-templated processes specifically and protein-protein interactions more generally in eukaryotes. The geminivirus movement protein NSP is essential for virus movement, shuttling the viral DNA genome between the nucleus and the cytoplasm. We have identified a novel Arabidopsis protein, AtNSI, that interacts with NSP. AtNSI is highly conserved among widely divergent plants. Biochemical studies show that its interaction with NSP is direct and that AtNSI acetylates histones, but not NSP, in vitro. Rather, AtNSI specifically acetylates the viral coat protein. AtNSI is a nuclear protein but does not act as a transcriptional coactivator in vitro, which distinguishes it from known eukaryotic histone acetyltransferases. Its overexpression enhances the efficiency of infection by Cabbage leaf curl virus. These findings suggest a role for protein acetylation in coordinating replication of the viral DNA genome with its export from the nucleus.

Citing Articles

Begomovirus-Host Interactions: Viral Proteins Orchestrating Intra and Intercellular Transport of Viral DNA While Suppressing Host Defense Mechanisms.

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RNA-seq analysis reveals an early defense response to tomato leaf curl New Delhi virus in potato cultivar Kufri Bahar.

Jeevalatha A, Siddappa S, Kumar R, Tiwari R, Lal M, Sharma S Funct Integr Genomics. 2023; 23(3):215.

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