The process of protein translation defines the ..
incorporated into the protein product of the gene
AAC is a membrane protein that acts like a revolving door - transporting ADP into mitochondria (to be converted to ATP) and ATP out of mitochondria and into the cytoplasm (Wang and Tajkhorshid 2008).
This lesson takes a look at tRNA and its role in protein synthesis
The translation of genetic information into proteins is essential forlife. At the core of this process lies the ribosome, a quintessentiallarge (2.5-4.5 MDa) molecular machine responsible for translatinggenetic material into functional proteins. In a growing cell, ribosomescomprise up to half of the net dry weight. Because of its fundamental rolein the cell, 50% of all efforts to develop antibiotics target bacterialribosomes, taking advantage of the structural differences between bacterialand human ribosomes.
Protein Synthesis -Translation and Regulation
Similar to TnaC described above, the peptide SecM exists solely to stallthe ribosome synthesizing it. But unlike TnaC, which also requires thepresence of high levels of trytophan, SecM has an intrinsic stallingcapability. Stalling of the ribosome synthesizing SecM provides time fora downstream RNA helix on the same mRNA strand to unwind. Unwinding ofthis helix then allows for a new ribosome to bind and synthesize anew protein, SecA, a bacterial ATP-driven translocase that aids the passage ofnascent proteins across membranes in conjunction with SecY (see also ). When sufficient levels of SecA have been reached,SecA interacts with the SecM-stalled ribosome to pull on SecM, freeingit and allowing translation to resume (illustrated schematically inFig. 13). SecM, which serves no otherpurpose than to stall the ribosome, is released into the cell anddegraded.
Drag-and-Drop Protein Synthesis: Translation - zeroBio
EF-Tu has three important regions that play a prominent role in itsGTPase activity: Switch I (EF-Tu residues 40--62; numbering)Switch II (80--100) and P-loop (18--23). All of these regions undergocharacteristic conformational changes in EF-Tu. Crystal structures ofEF-Tu in the GTP form display a "hydrophobic gate" formed by residuesVal20 (in the P-loop) and Ile60 (In Switch I) that controls access tothe GTP binding pocket. A schematic representation of this gate isshown in Fig 5A, the crystal structure shown in Fig. 5B. His84 (inSwitch II) needs to enter through this gate to perform its catalyticrole. Thus, this gate must be opened when the right codon-anticodoninteraction is recognized by the ribosome. A crystal structure of EF-Tuoutside the ribosome, but bound to the antibiotic aurodox that isthought to simulate interaction with the ribosome, displays an open gate(Fig. 5D). This antibiotic binds to EF-Tu and stimulates GTPaseactivity, preventing EF-Tu from binding the ribosome, and thereforepreventing translation and killing the cell. The fact that an open gateis found in the case of enhanced GTPase activity hints that thismechanism is used by the ribosome as well.