The IGBB logo features a stylized "pinwheel" to the left of the letters IGBB in caps in a modified Bank Gothic Pro font.
The six-part "pinwheel" in the IGBB logo is:
- A symbol of lab unity as it shows "parts" coming together to make a "whole."
- A flower or three-leaf clover representing (a) plants, important subjects of our research, (b) life in general, and (c) the life sciences (biology).
- A set of chromosomes being moved towards the center of a cell.
- The Sun - another symbol of life.
- A protein composed of six subunits (e.g., a protein pore).
- Three foxes putting their heads together. The fox is a symbol of cleverness in Western folklore. Since the IGBB is organized into three service groups (Genomics, Proteomics/Metabolomics, and Biocomputing/Computational Biology), the foxes could represent the three disciplines working together.
- A scientist jumping for joy after making an important discovery.
- A windmill, the primary symbol associated with Cervantes' famous character Don Quixote - Like Don Quixote, scientists must be willing to attack 'wicked giants' (e.g., ignorance, racism, sexism, intolerance, use of the term 'science' in the promotion of non-scientific causes), champion worthy causes (e.g., education, intellectual freedom, human rights, environmental responsibility), and remain optimistic in the face of defeat (e.g., most days in the lab). Hopefully, however, the average scientist can accomplish these tasks without becoming delusional (a problem that squashed Quixote's dreams of becoming a plant molecular biologist).
- A DNA double-helix or protein in cross section.
- Antibodies binding to a protein.
- Whatever you want it to be.
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:
99Nallamilli 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.
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The IGBB is an HPC² member center.