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Title: Crystal Structure of RNase T, an Exoribonuclease Involved in tRNA Maturation and End Turnover

Abstract

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.

Authors:
; ; ; ; ; ; ; ;
Publication Date:
Research Org.:
Brookhaven National Laboratory (BNL) National Synchrotron Light Source
Sponsoring Org.:
Doe - Office Of Science
OSTI Identifier:
930365
Report Number(s):
BNL-81084-2008-JA
Journal ID: ISSN 0969-2126; TRN: US200904%%653
DOE Contract Number:  
DE-AC02-98CH10886
Resource Type:
Journal Article
Resource Relation:
Journal Name: Structure; Journal Volume: 15
Country of Publication:
United States
Language:
English
Subject:
36 MATERIALS SCIENCE; CRYSTAL STRUCTURE; ENZYMES; ESCHERICHIA COLI; MONOMERS; MUTAGENESIS; PRECURSOR; PSEUDOMONAS; RESIDUES; RNA-ASE; SPECIFICITY; SUBSTRATES; national synchrotron light source

Citation Formats

Zuo,Y., Zheng, H., Wang, Y., Chruszcz, M., Cymborowski, M., Skarina, T., Savchenko, A., Malhotra, A., and Minor, W.. Crystal Structure of RNase T, an Exoribonuclease Involved in tRNA Maturation and End Turnover. United States: N. p., 2007. Web. doi:10.1016/j.str.2007.02.004.
Zuo,Y., Zheng, H., Wang, Y., Chruszcz, M., Cymborowski, M., Skarina, T., Savchenko, A., Malhotra, A., & Minor, W.. Crystal Structure of RNase T, an Exoribonuclease Involved in tRNA Maturation and End Turnover. United States. doi:10.1016/j.str.2007.02.004.
Zuo,Y., Zheng, H., Wang, Y., Chruszcz, M., Cymborowski, M., Skarina, T., Savchenko, A., Malhotra, A., and Minor, W.. Mon . "Crystal Structure of RNase T, an Exoribonuclease Involved in tRNA Maturation and End Turnover". United States. doi:10.1016/j.str.2007.02.004.
@article{osti_930365,
title = {Crystal Structure of RNase T, an Exoribonuclease Involved in tRNA Maturation and End Turnover},
author = {Zuo,Y. and Zheng, H. and Wang, Y. and Chruszcz, M. and Cymborowski, M. and Skarina, T. and Savchenko, A. and Malhotra, A. and Minor, W.},
abstractNote = {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.},
doi = {10.1016/j.str.2007.02.004},
journal = {Structure},
number = ,
volume = 15,
place = {United States},
year = {Mon Jan 01 00:00:00 EST 2007},
month = {Mon Jan 01 00:00:00 EST 2007}
}