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Hibernation factors can do a variety of things, including dismantling cellular machinery and halting gene expression, but the most important hibernation factors bind to the ribosome and halt protein production, which consumes a large fraction of the energy in a cell. [1] [2] How different hibernation factors bind to the ribosome's active sites
For instance, in E. coli, 70S ribosomes form 90S dimers upon binding with a small 6.5 kDa protein, ribosome modulation factor RMF. [ 18 ] [ 19 ] These intermediate ribosome dimers can subsequently bind a hibernation promotion factor (the 10.8 kDa protein, HPF) molecule to form a mature 100S ribosomal particle, in which the dimerization ...
Overview of eukaryotic messenger RNA (mRNA) translation Translation of mRNA and ribosomal protein synthesis Initiation and elongation stages of translation involving RNA nucleobases, the ribosome, transfer RNA, and amino acids The three phases of translation: (1) in initiation, the small ribosomal subunit binds to the RNA strand and the initiator tRNA–amino acid complex binds to the start ...
Ribosome profiling experiments have shown that TF predominantly targets ribosomes translating outer membrane proteins in vivo, and moreover are underrepresented on ribosomes translating inner membrane proteins. [11] Trigger factor not only directly works to properly fold the protein but also recruits other chaperones to the ribosome, such as Hsp70.
The tRNA first binds to the ribosome like a tRNA, then with SmpB's help shifts into the mRNA position to translate a short peptide ending on a normal stop codon. [4] Alternative ribosome-rescue factor A (ArfA) is an alternative system in E. coli. It recruits RF2. [4] Alternative ribosome-rescue factor B (ArfB) is another alternative from E. coli.
The ribosome can localize to the start site by direct binding, initiation factors, and/or ITAFs (IRES trans-acting factors) bypassing the need to scan the entire 5' UTR. This method of translation is important in conditions that require the translation of specific mRNAs during cellular stress, when overall translation is reduced.
Ribosome recycling factor or ribosome release factor (RRF) is a protein found in bacterial cells as well as eukaryotic organelles, specifically mitochondria and chloroplasts. It functions to recycle ribosomes after completion of protein synthesis ( bacterial translation ).
The IF2 initiation factor is a crucial component in the process of protein synthesis. The largest among the three indispensable translation initiation factors is IF-2, which possesses a molecular mass of 97 kDa. [17] [18] The protein has many domains, including an N-terminal domain, a GTPase domain, a linker region, C1, C2, and C-terminal domains.