Volume 45, Issue 4
28 February 2017
NAR Breakthrough Article
SURVEY AND SUMMARY
Chemical Biology and Nucleic Acid Chemistry
Data Resources and Analyses
Gene Regulation, Chromatin and Epigenetics
Genome Integrity, Repair and Replication
Nucleic Acid Enzymes
Identification of 2-methylthio cyclic N6-threonylcarbamoyladenosine (ms2ct6A) as a novel RNA modification at position 37 of tRNAs
Byeong-il Kang; Kenjyo Miyauchi; Michal Matuszewski; Gabriel Silveira D'Almeida; Mary Anne T. Rubio ...
Synthetic Biology and Bioengineering
GB3.0: a platform for plant bio-design that connects functional DNA elements with associated biological data
Marta Vazquez-Vilar; Alfredo Quijano-Rubio; Asun Fernandez-del-Carmen; Alejandro Sarrion-Perdigones; Rocio Ochoa-Fernandez ...
Cover ImageCover: RNA-induced movement of the RNA-binding domain of YxiN. Superposition of the final structural models for YxiN in the absence and presence of RNA on the helicase core (gray). Models were obtained from FRET-restrained modeling (left: back view, right: front view). The position of the RNA-binding domain (RRM) in the absence of RNA is shown in pale cyan, in the presence of RNA it is depicted in blue. The YxiN helicase core (dark gray: N-terminal RecA domain, RecA_N, light gray: C-terminal RecA domain, RecA_C) carrying the mutations S108C (red) and D262C (orange) in the open state is a homology model, generated using mjDEAD (PDB-ID 1hv8) as a template. The RRM containing cysteines at positions 429, 444, 464 and 472 (yellow), was modeled with the structure of the YxiN RRM (PDB-ID 2goc) as template. RNA binding to the YxiN RRM causes a large movement of the RRM from a position close to RecA_C of the helicase core towards RecA_N.
For more information see article by Samatanga, B. et al., pages 1994–2006 in this issue.
- Front Matter
- Table of Contents