Crystal structure of RNase T, an exoribonuclease involved in tRNA maturation and end turnover.
The 3' processing of most bacterial precursor tRNAs involves exonucleolytic trimming to yield a mature CCA end. This step is carried out by RNase T, a member of the large DEDD family of exonucleases. We report the crystal structures of RNase T from Escherichia coli and Pseudomonas aeruginosa, which show that this enzyme adopts an opposing dimeric arrangement, with the catalytic DEDD residues from one monomer closely juxtaposed with a large basic patch on the other monomer. This arrangement suggests that RNase T has to be dimeric for substrate specificity, and agrees very well with prior site-directed mutagenesis studies. The dimeric architecture of RNase T is very similar to the arrangement seen in oligoribonuclease, another bacterial DEDD family exoribonuclease. The catalytic residues in these two enzymes are organized very similarly to the catalytic domain of the third DEDD family exoribonuclease in E. coli, RNase D, which is monomeric.
Zuo
Yuhong
Y
Department of Biochemistry and Molecular Biology, University of Miami School of Medicine, Miami, FL 33101, USA.
Zheng
Heping
H
Wang
Yong
Y
Chruszcz
Maksymilian
M
Cymborowski
Marcin
M
Skarina
Tatiana
T
Savchenko
Alexei
A
Malhotra
Arun
A
Minor
Wladek
W
D000595:Amino Acid Sequence; D004926:Escherichia coli / Q000201:enzymology / Q000235:genetics; D005095:Exoribonucleases / Q000737:chemistry* / Q000235:genetics; D008969:Molecular Sequence Data; D011550:Pseudomonas aeruginosa / Q000201:enzymology / Q000235:genetics; D012343:RNA, Transfer / Q000737:chemistry* / Q000378:metabolism
D012343:RNA, Transfer; D005095:Exoribonucleases; C042081:exoribonuclease T