Interrupted Catalysis: The EF4 (LepA) Effect on Back-Translocation
نویسندگان
چکیده
منابع مشابه
Taking a Step Back from Back-Translocation: an Integrative View of LepA/EF4's Cellular Function.
Protein synthesis, the translation of mRNA into a polypeptide facilitated by the ribosome, is assisted by a variety of protein factors, some of which are GTPases. In addition to four highly conserved and well-understood GTPases with known function, there are also a number of noncanonical GTPases that are implicated in translation but whose functions are not fully understood. LepA/EF4 is one of ...
متن کاملThe conserved protein EF4 (LepA) modulates the elongation cycle of protein synthesis.
EF4 (LepA), a strongly conserved protein, is important for bacterial growth and functional protein biosynthesis under certain conditions and is quite similar structurally to the translocase EF-G. The elongation cycle in protein synthesis is characterized by ribosome oscillation between pretranslocation (PRE) and posttranslocation (POST) complexes. Here, using ensemble single turnover and equili...
متن کاملRibosomal Translocation: LepA Does It Backwards
During translation, mRNA is threaded through the ribosome in precise and directional three-nucleotide steps. A recent paper identifies a new GTPase, LepA, which catalyzes unexpected one-codon backward movement on the ribosome.
متن کاملElongation factor 4 (EF4/LepA) accelerates protein synthesis at increased Mg2+ concentrations.
Elongation factor 4 (EF4) is one of the most conserved proteins present in bacteria as well as in mitochondria and chloroplasts of eukaryotes. Although EF4 has the unique ability to catalyze the back-translocation reaction on posttranslocation state ribosomes, the physiological role of EF4 remains unclear. Here we demonstrate that EF4 is stored at the membrane of Escherichia coli cells and rele...
متن کاملThe structure of LepA, the ribosomal back translocase.
LepA is a highly conserved elongation factor that promotes the back translocation of tRNAs on the ribosome during the elongation cycle. We have determined the crystal structure of LepA from Escherichia coli at 2.8-A resolution. The high degree of sequence identity between LepA and EF-G is reflected in the structural similarity between the individual homologous domains of LepA and EF-G. However,...
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ژورنال
عنوان ژورنال: Journal of Molecular Biology
سال: 2010
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2009.12.043