lepA Antibody, Biotin conjugated

1. The last 44 C-terminal amino acids of EF4 form a sub-domain within the C-terminal domain that is important for GTP-dependent function on the ribosome. PMID: 25712150
2. Thus, EF4 has two opposing functions-at low-to-moderate levels of stress, the protein is protective by allowing stress-paused translation to resume; at high-levels of stress, EF4 helps bacteria self-destruct. PMID: 25491353
3. (review) EF4 triggers back-translocation of the elongating ribosome, causing the translation machinery to move one codon backwards along the mRNA. PMID: 23662805
4. Elevated intracellular Mg(2+) concentrations or low temperature inhibit protein synthesis, probably because of formation of aberrant elongating ribosomal states. We suggest that EF4 binds to these stuck ribosomes and remobilizes them PMID: 21300907
5. EF4-dependent back-translocation proceeds from a post-translocation (POST) complex to a pre-translocation (PRE) complex via a four-step kinetic scheme (i.e., POST-->I(1)-->I(2)-->I(3)-->PRE PMID: 20045415
6. LepA protein, present in all bacteria and mitochondria, is a third elongation factor required for accurate and efficient protein synthesis. PMID: 17110332
7. The crystal structure of LepA from Escherichia coli at 2.8-A resolution, was determined. PMID: 18362332

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KEGG: ecj:JW2553

STRING: 316385.ECDH10B_2737