ABC-F proteins in mRNA translation and antibiotic resistance |
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Affiliation: | 1. UMR 8261, CNRS, Université de Paris, Institut de Biologie Physico-Chimique, 75005, Paris, France;2. Department of Biological, 702A Sherman Fairchild Center, Columbia University, New York, NY, 10027, United States;3. Département de Microbiologie, Institut Pasteur, 75724, Paris Cedex 15, France;1. Laboratory of Membrane Biology and Biophysics, The Rockefeller University, New York, NY 10065, USA;2. Howard Hughes Medical Institute, The Rockefeller University, New York, NY 10065, USA |
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Abstract: | The ATP binding cassette protein superfamily comprises ATPase enzymes which are, for the most part, involved in transmembrane transport. Within this superfamily however, some protein families have other functions unrelated to transport. One example is the ABC-F family, which comprises an extremely diverse set of cytoplasmic proteins. All of the proteins in the ABC-F family characterized to date act on the ribosome and are translation factors. Their common function is ATP-dependent modulation of the stereochemistry of the peptidyl transferase center (PTC) in the ribosome coupled to changes in its global conformation and P-site tRNA binding geometry. In this review, we give an overview of the function, structure, and theories for the mechanisms-of-action of microbial proteins in the ABC-F family, including those involved in mediating resistance to ribosome-binding antibiotics. |
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Keywords: | ABC superfamily ABC-F protein family mRNA translation Translation regulation Antibiotic resistance ATPase PTC" },{" #name" :" keyword" ," $" :{" id" :" kwrd0045" }," $$" :[{" #name" :" text" ," _" :" peptidyl transferase center NPET" },{" #name" :" keyword" ," $" :{" id" :" kwrd0055" }," $$" :[{" #name" :" text" ," _" :" nascent peptide exit tunnel A/P/E-sites" },{" #name" :" keyword" ," $" :{" id" :" kwrd0065" }," $$" :[{" #name" :" text" ," _" :" ribosomal Acceptor (A), peptidyl (P), exit (E) sites Cryo-EM" },{" #name" :" keyword" ," $" :{" id" :" kwrd0075" }," $$" :[{" #name" :" text" ," _" :" Cryo-electron microscopy |
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