This work intends to survey specific RNAs associated with isolated membrane systems of cultured human cells. These RNAs are identified with specific sequences by array hybridization and massed sequencing. Identihed individual membrane-associated RNAs are subsequently screened for binding to purified phospholipid bilayers with the composition of human membranes, in the presence and absence of proteins. Residence on cellular membran es in vivo for RNAs with these biochemical properties is confirmed using FRET between RNA-complementary fluorescent oligonucleotides and membrane dyes introduced into living cells. The intended net effect ofthese three protocols is to detect a subset of membrane-resident RNAs in human cells that have bilayer affinity built into their covalent structures,

Public Health Relevance

This work seeks to define and elucidate membrane-RNA interactions in which RNA molecules and membrane lipids associate without the intervention of other molecules. Given that this interaction occurs in human cells, previously unrecognized causes of wellbeing and disease will exist in correct or misdirected membrane-RNA interactions. Thus basic biology with biomedical implications is proposed, potentially illuminating a previously unrecognized class of health-related cellular events.

Agency
National Institute of Health (NIH)
Institute
National Institute of General Medical Sciences (NIGMS)
Type
Research Project (R01)
Project #
1R01GM082917-01A1
Application #
7522472
Study Section
Special Emphasis Panel (ZRG1-CB-M (90))
Program Officer
Preusch, Peter C
Project Start
2009-09-30
Project End
2011-08-31
Budget Start
2009-09-30
Budget End
2010-08-31
Support Year
1
Fiscal Year
2009
Total Cost
$284,529
Indirect Cost
Name
University of Colorado at Boulder
Department
Biochemistry
Type
Schools of Arts and Sciences
DUNS #
007431505
City
Boulder
State
CO
Country
United States
Zip Code
80309
Turk-Macleod, Rebecca M; Puthenvedu, Deepa; Majerfeld, Irene et al. (2012) The plausibility of RNA-templated peptides: simultaneous RNA affinity for adjacent peptide side chains. J Mol Evol 74:217-25