Proteins arginine residues

PAD4 is a Ca -dependent enzyme that catalyzes the conversion of protein arginine residues to citrulline. (a) Ribbon representation of the PAD4/benzoyl-L-arginine amide complex (PDB code Iwda) in the presence of the ions (green spheres). 

GTP-binding protein at an arginine residue which is involved in GTP hydrolysis. ADP-ribosylation thus leads to constitutive activation of Gs. 

Histones are small, basic proteins required to condense DNA into chromatin. They have been first described and named in 1884 by Albrecht Kossel. There are five main histones HI, H2A, H2B, H3 andH4. An octamer of core histones H2A, H2B, H3 andH4 is located inside a nucleosome, the central building block of chromatin, with about 150 base pairs of DNA wrapped around. The basic nature of histones, mediated by the high content of lysine and arginine residues, allows a direct interaction with the acidic phosphate back bone of DNA. The fifth histone HI is located outside at the junction between nucleosomes and is referred to as the linker histone. Besides the main histones, so-called histone variants are known, which replace core histones in certain locations like centromers. 

All rhodopsin-like G-protein-coupled receptors have a conserved arginine residue at the intracellular end of TM3 and this residue is thought to be crucial for G-protein activation. The third intracellular loop determines the class of G-protein activated by the receptor with the second intracellular loop and C-terminus also influencing G-protein binding in some cases. Four classes of G-protein are known ... 

Figure 5.37 APG can be used to label specifically arginine residues in proteins, producing stable, cyclic Schiff base-like bonds with the side-chain guanidino groups. Photoactivation with UV light then causes ring expansion of the phenyl azide group, initiating covalent bond formation with amines.

Takahashi, K. (1968) The reaction of phenylglyoxal with arginine residues in proteins. J. Biol. Chem. 243, 6171-6179. 

Yamasaki, R.B., Shimcr, D.A., and Feeney, R.E. (1981) Colorimetric determination of arginine residues in proteins by p-nitrophenylglyoxal. Anal. Biochem. Ill, 220. 

Cholera toxin catalyzes the ADP-ribosylation of a specific arginine residue in G and Gat. This covalent modification inhibits the intrinsic GTPase activity of these a subunits and thereby freezes them in their activated, or free, state (Fig. 19-1C). By this mechanism, cholera toxin stimulates adenylyl cyclase activity and photoreceptor transduction mechanisms. The ability of cholera toxin to ADP-ribosylate G may require the presence of a distinct protein, ADP-ribosylation factor (ARF). ARF, which is itself a small G protein (Table 19-2), also is ADP-ribosylated by cholera toxin. ARF is implicated in controlling membrane vesicle trafficking (see Ch. 9). 

Figure 3.2 Ribbon diagram of the C-lobe of human transferrin with the two domains shown in different colours (cyan for Cl and green for C2). The inset shows the four protein ligand residues together with the arginine residue which stabilizes binding of the synergistic carbonate ion (both in magenta). (Reprinted with permission from Mason et al., 2005. Copyright (2005) American Chemical Society.)...

For the residue-type assignment of the cross peaks, the SH3 domain was expressed with specifically labeled glycine or arginine residues by using amino acid mixtures where only Gly and Arg were 15N-labeled. Again, yields for the labeled proteins were identical to those of the unlabeled product. Analysis of the corresponding [15N,1H]-HSQC spectra... 

Harris R.J. (1995), Processing of C-terminal lysine and arginine residues of proteins isolated from mammalian cell culture, J. Chromatogr. A 705(1) 129-134. 

The bacterium Pseudomonas aeruginosa produces several virulence factors. In particular ExoS has an ADP-ribosylation domain that affects arginine residues. When pleotypic cells are infected with ExoS, the phosphorylation of ezrin/radixin/moesin (ERM) proteins no longer occurs." It happens that ERM proteins are high-afifmity substrates for the ADP-ribosylation domain of ExoS. When the sequence of moesin was... 

A protein identification study might proceed in the following manner. Pirst, the protein is analyzed by mass spectrometry to determine its molecular mass to within 0.01%. Second, the protein is digested with an enzyme, commonly trypsin. The enzyme trypsin cleaves polypeptide chains at points following lysine and arginine residues. Using this proteolytic enzyme ensures that each... 

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