Molecular basis of inhibition of the ribonuclease activity in colicin E5 by its cognate immunity protein

Journal of Molecular Biology
César Luna-ChávezRaven H Huang

Abstract

Colicin E5 is a tRNA-specific ribonuclease that recognizes and cleaves four tRNAs in Escherichia coli that contain the hypermodified nucleoside queuosine (Q) at the wobble position. Cells that produce colicin E5 also synthesize the cognate immunity protein (Im5) that rapidly and tightly associates with colicin E5 to prevent it from cleaving its own tRNAs to avoid suicide. We report here the crystal structure of Im5 in a complex with the activity domain of colicin E5 (E5-CRD) at 1.15A resolution. The structure reveals an extruded domain from Im5 that docks into the recessed RNA binding cleft in E5-CRD, resulting in extensive interactions between the two proteins. The interactions are primarily hydrophilic, with an interface that contains complementary surface charges between the two proteins. Detailed interactions in three separate regions of the interface account for specific recognition of colicin E5 by Im5. Furthermore, single-site mutational studies of Im5 confirmed the important role of particular residues in recognition and binding of colicin E5. Structural comparison of the complex reported here with E5-CRD alone, as well as with a docking model of RNA-E5-CRD, indicates that Im5 achieves its inhibition by physically block...Continue Reading

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Citations

Nov 17, 2011·Quarterly Reviews of Biophysics·Grigorios PapadakosColin Kleanthous
Dec 14, 2012·Proceedings of the National Academy of Sciences of the United States of America·Robert P MorseCelia W Goulding
Jul 21, 2012·Journal of Biochemistry·Sakura Inoue-ItoHaruhiko Masaki
Mar 10, 2007·Microbiology and Molecular Biology Reviews : MMBR·Eric CascalesDanièle Cavard
Mar 12, 2016·Bioscience, Biotechnology, and Biochemistry·Tetsuhiro Ogawa
Jan 27, 2007·FEMS Microbiology Reviews·Javier LacadenaAlvaro Martínez del Pozo
Apr 22, 2014·Biochimica Et Biophysica Acta·Young Chan KimChristopher N Penfold

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