Arrestins have emerged as one family of proteins that mediate the inactivation of G-protein-coupled receptors. We have isolated cDNA clones encoding two arrestin isoforms of the dipteran visual system, Calliphora arrestin 1 (Arr1) and arrestin 2 (Arr2). Microsequencing established that the arr2 gene encodes the Calliphora 49-kDa protein characterized previously as a photoreceptor-specific prote...

The aim of this work was to search for the biological function of protein isoprenylation. For this purpose, peptides were synthesized and, by using a convenient protocol, were farnesylated or geranylated at the thiol group of the C-terminal cysteine. The interaction of these peptides with photoactivated rhodopsin (Rho*, which is functionally equivalent to metarhodopsin II) was studied with the ...

G protein-coupled receptors (GPCRs) are seven transmembrane domain proteins that transduce extracellular signals across the plasma membrane and couple to the heterotrimeric family of G proteins. Like most intrinsic membrane proteins, GPCRs are capable of oligomerization, the function of which has only been established for a few different receptor systems. One challenge in understanding the func...

We report high resolution solution (19)F NMR spectra of fluorine-labeled rhodopsin mutants in detergent micelles. Single cysteine substitution mutants in the cytoplasmic face of rhodopsin were labeled by attachment of the trifluoroethylthio (TET), CF(3)-CH(2)-S, group through a disulfide linkage. TET-labeled cysteine mutants at amino acid positions 67, 140, 245, 248, 311, and 316 in rhodopsin w...

Title of Document: RNAI AND MORPHOLINO AS TOOLS TO STUDY SIGNALING IN LIMULUS VENTRAL PHOTORECEPTORS. Monika M Deshpande, Doctor of Philosophy, 2006 Directed By: Dr. Richard Payne, Neuroscience and Cognitive Science program Limulus ventral photoreceptors have been studied using electrophysiological, immunocytochemical, and biochemical techniques. However, genetic manipulation has eluded Limulus...

Light activated rhodopsin interacts with domains on all three subunits of transducin. Two of these domains, the C-terminal regions of the alpha and gamma subunits mimic the ability of transducin to stabilize the active conformation of rhodopsin, metarhodopsin II, but display different roles in transducin activation process. Whether the interactions are with the same or different complimentary s...

The effects of ionic strength on formation and decay of metarhodopsin II (MII), the active photointermediate of bovine rhodopsin, were studied in the native membrane environment by means of ultraviolet/ visible and Fourier-transform infrared (FTIR) spectroscopy. By increasing the concentration of KCl in the range from hypotonic to 4 M, the apparent pKa of the metarhodopsin I(MI)/MII equilibrium...