scholarly journals Sequence Specific RNA Recognition Mechanism of MazF

2015 ◽  
Vol 55 (1) ◽  
pp. 011-014
Author(s):  
Yoshihiro YAMAGUCHI
2020 ◽  
Vol 477 (1) ◽  
pp. 161-172 ◽  
Author(s):  
Kaiyue Qian ◽  
Mengyu Li ◽  
Junchao Wang ◽  
Min Zhang ◽  
Mingzhu Wang

RNA-binding protein RBM38 was reported to bind the mRNA of several p53-related genes through its RRM domain and to up-regulate or down-regulate protein translation by increasing mRNA stability or recruitment of other effector proteins. The recognition mechanism, however, for RNA-binding of RBM38 remains unclear. Here, we report the crystal structure of the RRM domain of human RBM38 in complex with a single-stranded RNA. Our structural and biological results revealed that RBM38 recognizes G(U/C/A)GUG sequence single-stranded RNA in a sequence-specific and structure-specific manner. Two phenylalanine stacked with bases of RNA were crucial for RNA binding, and a series of hydrogen bonds between the base atoms of RNA and main-chain or side-chain atoms of RBM38 determine the sequence-specific recognition. Our results revealed the RNA-recognition mechanism of human RBM38 and provided structural information for understanding the RNA-binding property of RBM38.


2009 ◽  
Vol 37 (15) ◽  
pp. 5151-5166 ◽  
Author(s):  
Kengo Tsuda ◽  
Kanako Kuwasako ◽  
Mari Takahashi ◽  
Tatsuhiko Someya ◽  
Makoto Inoue ◽  
...  

Science ◽  
2010 ◽  
Vol 329 (5997) ◽  
pp. 1355-1358 ◽  
Author(s):  
Rachel E. Haurwitz ◽  
Martin Jinek ◽  
Blake Wiedenheft ◽  
Kaihong Zhou ◽  
Jennifer A. Doudna

Many bacteria and archaea contain clustered regularly interspaced short palindromic repeats (CRISPRs) that confer resistance to invasive genetic elements. Central to this immune system is the production of CRISPR-derived RNAs (crRNAs) after transcription of the CRISPR locus. Here, we identify the endoribonuclease (Csy4) responsible for CRISPR transcript (pre-crRNA) processing in Pseudomonas aeruginosa. A 1.8 angstrom crystal structure of Csy4 bound to its cognate RNA reveals that Csy4 makes sequence-specific interactions in the major groove of the crRNA repeat stem-loop. Together with electrostatic contacts to the phosphate backbone, these enable Csy4 to bind selectively and cleave pre-crRNAs using phylogenetically conserved serine and histidine residues in the active site. The RNA recognition mechanism identified here explains sequence- and structure-specific processing by a large family of CRISPR-specific endoribonucleases.


Biochemistry ◽  
2009 ◽  
Vol 48 (20) ◽  
pp. 4314-4323 ◽  
Author(s):  
Takashi Matsui ◽  
Takeshi Tanaka ◽  
Hiroshi Endoh ◽  
Kazuki Sato ◽  
Hidekazu Tanaka ◽  
...  

2007 ◽  
Vol 141 (2) ◽  
pp. 269-277 ◽  
Author(s):  
Takashi Matsui ◽  
Yoshio Kodera ◽  
Hiroshi Endoh ◽  
Emi Miyauchi ◽  
Hiroyoshi Komatsu ◽  
...  

FEBS Letters ◽  
2007 ◽  
Vol 581 (8) ◽  
pp. 1599-1604 ◽  
Author(s):  
Keisuke Matsumoto ◽  
Takashi Toyooka ◽  
Chie Tomikawa ◽  
Anna Ochi ◽  
Yoshitaka Takano ◽  
...  

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