C-terminus of protein

PPCs Prenylation is the post-translational addition of 15- or 20-carbon isoprenyl lipids to the C-terminus of proteins. Prenylation is an irreverable modification that anchors proteins to the membrane fraction of cells. 

Ribosomal Protein Synthesis Inhibitors. Figure 4 The binding site of pactamycin on the 30S subunit. The positions of mRNA, the RNA elements H28, H23b, H24a, and the C-terminus of protein S7 are depicted in the E-site of the native 30S structure (left) and in the 30S-pactamycin complex (right). In the complex with pactamycin, the position of mRNA is altered (from Brodersen etal. [4] with copyright permission). 

Nemoto, N., Miyamoto-Sato, E., and Yanagawa, H., Fluorescence labeUng of the C-terminus of proteins with a puromycin analogue in ceU-free translation systems, FEBS Lett., 462,1-2,43,1999. 

The GAL4 recognition module therefore contains only one protein side chain, Lys 18, that provides specific interactions with the DNA. The remaining specific interactions with DNA are from main-chain atoms and depend critically on the correct conformation of the protein. The correct positioning of the C-terminus of the a helix is particularly important for recognition. This is to date the only example of a protein-DNA interaction in which... 

Figure 16.21 Structure of one subunit of the core protein of Slndbls virus. The protein has a similar fold to chymotrypsin and other serine proteases, comprising two Greek key motifs separated by an active site cleft. The C-terminus of the protein is bound in the catalytic site, making the coat protein inactive (Adapted from S. Lee et al., Structure 4 531-541, 1996.)...

The farnesylation and subsequent processing of the Ras protein. Following farnesylation by the FTase, the carboxy-terminal VLS peptide is removed by a prenyl protein-specific endoprotease (PPSEP) in the ER, and then a prenylprotein-specific methyltransferase (PPSMT) donates a methyl group from S-adenosylmethionine (SAM) to the carboxy-terminal S-farnesylated cysteine. Einally, palmitates are added to cysteine residues near the C-terminus of the protein. 

An exopeptidase that sequentially releases an amino from the C-terminus of a protein or peptide. Carbox-ypeptidases are classified in Enzyme Nomenclature according to catalytic type and are included in subsubclasses 3.4.16-3.4.18. 

The presence of chromosomal translocations is a consistent feature of many leukemia s, lymphomas, and certain solid tumors. At the genetic level, these events can either deregulate an intact gene by disruption or removal and replacement of the adjacent controlling elements, or create a new fusion gene that express the N-terminus of one protein fused to the C-terminus of another protein. 

In addition SENPs are required for maturation of SUMO precursors. SUMO proteins are translated as inactive precursors with a short C-terminal prosequence of variable length. This sequence needs to be removed to expose a double glycine motif at the C-terminus of SUMO that is required for conjugation. 

Toll/IL-l receptor domain - A domain found on the internal C-terminus of Toll-like receptors involved in binding the adapter proteins to initiate signalling inside the cell. 

Several studies were performed on the optimization of expression levels of ELP proteins in E. coli. In a recent example, the expression protocol was optimized for an ELP fusion with green fluorescent protein (GFP). This fusion protein was expressed and purified in a yield of 1.6 g/L of bacterial culture, which finally yielded 400 mg GFP/L bacterial culture. This extremely high yield was found after uninduced expression in nutrient-rich medium supplemented with phosphate, glycerol and certain amino acids, such as proline and alanine [234]. The influence of fusion order was also examined and it was found that positioning the ELP at the C-terminus of target protein resulted in significantly higher expression levels [35]. 

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