The IGBB is a member of the NIH-funded Mississippi IDeA Network of Biomedical Research Excellence (Mississippi INBRE or MS-INBRE), a program designed to build biomedical infrastructure throughout the state. Through MS-INBRE, Mississippi students and faculty at Mississippi's undergraduate institutions are (1) trained in biomedical research techniques, (2) given the opportunity to work with top researchers at Mississippi's major research universities, (3) afforded access to state-of-the-art bioscience equipment, and (4) provided with assistance in preparing grant proposals. The IGBB serves as the MS-INBRE proteomics/computational biology core. For more information about MS-INBRE, click here.
Dr. George V. PopescuAssistant Research Professor
FACULTY
email(662) 325-7369
Pace 118
Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa)
IGBB Authors:
Babi R.R. Nallamilli, Mariola J. Edelmann, Hana Mujahid, Zhaohua PengPUBLICATION YEAR:
2014IMPACT FACTOR:
4.005CITATION COUNT:
102Nallamilli BR, Edelmann MJ, Zhong X, Tan F, Mujahid H, Zhang J, Nanduri B, Peng Z (2014) Global analysis of lysine acetylation suggests the involvement of protein acetylation in diverse biological processes in rice (Oryza sativa).
PLoS One 9(2): e89283.
DOI:
10.1371/journal.pone.0089283EID:
2-s2.0-84895895875PMID: 24586658
DOWNLOAD PDFABSTRACTLysine acetylation is a reversible, dynamic protein modification regulated by lysine acetyltransferases and deacetylases. Recent advances in high-throughput proteomics have greatly contributed to the success of global analysis of lysine acetylation. A large number of proteins of diverse biological functions have been shown to be acetylated in several reports in human cells, E.coli, and dicot plants. However, the extent of lysine acetylation in non-histone proteins remains largely unknown in monocots, particularly in the cereal crops. Here we report the mass spectrometric examination of lysine acetylation in rice (Oryza sativa). We identified 60 lysine acetylated sites on 44 proteins of diverse biological functions. Immunoblot studies further validated the presence of a large number of acetylated non-histone proteins. Examination of the amino acid composition revealed substantial amino acid bias around the acetylation sites and the amino acid preference is conserved among different organisms. Gene ontology analysis demonstrates that lysine acetylation occurs in diverse cytoplasmic, chloroplast and mitochondrial proteins in addition to the histone modifications. Our results suggest that lysine acetylation might constitute a regulatory mechanism for many proteins, including both histones and non-histone proteins of diverse biological functions.
The IGBB is supported, in part, by the following units:
The IGBB is an HPC² member center.
