While the IGBB Service Center can perform low-risk, fairly routine biomolecular tasks on a fee-per-service basis, some of your research goals may require (or would most readily be completed with) the help of professionals trained in advanced procedures and/or data analysis techniques. The IGBB research associates, most of whom have Ph.D. degrees and/or many years of practical experience, can be hired to conduct research tasks associated with their specialties. For example, let's say you need an expert in RNA isolation and RNAseq to help you complete a portion of a research project. You could train a student or postdoc to become proficient in these research tasks, but you may not have the experience, time, or money to train someone. Moreover, you may not have the instrumentation you need to do the research correctly. This is where the IGBB can help. Rather than training someone new, you can hire a highly skilled IGBB scientist to perform the research for you. The savings in cost and time is tremendous! The process works like this:
- The principal investigator (PIs) interested in determining whether
the IGBB can help them in their research/analyses contacts one of the IGBB's Research Leads.
- The Research Lead(s) sets up a meeting with the PI to discuss project goals, feasibility, and
approaches. This consultation is free.
- If the PI and the Research Lead agree to a research plan, the
Research Lead
will generate an itemized quote for the PI that includes salary, fringe, reagent
costs, machine costs, etc. The duration of the employment agreement depends upon the needs of the customer and can range from a few hours to several months. In addition, IGBB employment agreements can cover fairly low weekly time committments spread out over long stretches (e.g., a customer may hire an IGBB employee to work on a project 5 hours a week for four years). Overhead charges and/or HPC² retainage costs may or may not be
applicable. Once a plan is set between a PI and an IGBB Research Lead, a final quote will be sent to the PI for approval. Once the PI approves the quote, work can begin.
If you don't have funding in hand, but are working on a grant proposal, you can include the participation of an IGBB expert-for-hire in your proposal budget (note: you must make such agreements with the expert-for-hire through a MyIGBB itemized quote). To discuss a hiring an IGBB expert, please contact one of the IGBB's Research Leads by phone or e-mail.
NOTE: PIs are asked to consider whether the participation of an IGBB employee in a project merits that employee's inclusion as a co-author on a resulting manuscript(s). The decision ultimately lies with the PI. However, the IGBB encourages IGBB staff and faculty involved in
Proposal Partnerships and
Experts for Hire to discuss/negotiate co-authorship with PIs before starting work on a project.

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:
100Nallamilli 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.
Dr. Daniel G. Peterson (Dan)Director & Professor
DIRECTOR
email(662) 325-2747
Portera 131A
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