Abstract:
:Ribosomal protection proteins (RPPs) confer bacterial resistance to tetracycline by releasing this antibiotic from ribosomes stalled in protein synthesis. RPPs share structural similarity to elongation factor G (EF-G), which promotes ribosomal translocation during normal protein synthesis. We constructed and functionally characterized chimeric proteins of Campylobacter jejuni Tet(O), the best characterized RPP, and Escherichia coli EF-G. A distinctly conserved loop sequence at the tip of domain 4 is required for both factor-specific functions. Domains 3-5: (i) are necessary, but not sufficient, for functional specificity; and (ii) modulate GTP hydrolysis by EF-G, while minimally affecting Tet(O), under substrate turnover conditions.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Thakor NS,Nechifor R,Scott PG,Keelan M,Taylor DE,Wilson KSdoi
10.1016/j.febslet.2008.03.023subject
Has Abstractpub_date
2008-04-16 00:00:00pages
1386-90issue
9eissn
0014-5793issn
1873-3468pii
S0014-5793(08)00252-4journal_volume
582pub_type
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