RraA: a Protein Inhibitor of RNase E Activity that Globally Modulates RNA Abundance in E. coli Export

@article{citeulike:532477, abstract = {Ribonuclease E (RNase E) has a key role in mRNA degradation and the processing of catalytic and structural RNAs in E. coli. We report the discovery of an evolutionarily conserved 17.4 kDa protein, here named RraA (regulator of ribonuclease activity A) that binds to RNase E and inhibits RNase E endonucleolytic cleavages without altering cleavage site specificity or interacting detectably with substrate RNAs. Overexpression of RraA circumvents the effects of an autoregulatory mechanism that normally maintains the RNase E cellular level within a narrow range, resulting in the genome-wide accumulation of RNase E-targeted transcripts. While not required for RraA action, the C-terminal RNase E region that serves as a scaffold for formation of a multiprotein degradosome complex modulates the inhibition of RNase E catalytic activity by RraA. Our results reveal a possible mechanism for the dynamic regulation of RNA decay and processing by inhibitory RNase binding proteins.}, author = {Lee, Kangseok and Zhan, Xiaoming and Gao, Junjun and Qiu, Ji and Feng, Yanan and Meganathan, R. and Cohen, Stanley N. and Georgiou, George}, citeulike-article-id = {532477}, citeulike-linkout-0 = {http://dx.doi.org/10.1016/j.cell.2003.08.003}, citeulike-linkout-1 = {http://www.sciencedirect.com/science/article/B6WSN-49JG1GK-C/2/3f0a0c7b7f7fb797c931494c00340ddc}, day = {5}, doi = {10.1016/j.cell.2003.08.003}, journal = {Cell}, keywords = {1q5x, alphabeta, rnasee\_inhibitor, s\_h}, month = {September}, number = {5}, pages = {623--634}, posted-at = {2006-03-07 14:03:34}, priority = {2}, title = {RraA: a Protein Inhibitor of RNase E Activity that Globally Modulates RNA Abundance in E. coli}, url = {http://dx.doi.org/10.1016/j.cell.2003.08.003}, volume = {114}, year = {2003} }

TY - JOUR ID - citeulike:532477 L3 - citeulike-article-id:532477 N2 - Ribonuclease E (RNase E) has a key role in mRNA degradation and the processing of catalytic and structural RNAs in E. coli. We report the discovery of an evolutionarily conserved 17.4 kDa protein, here named RraA (regulator of ribonuclease activity A) that binds to RNase E and inhibits RNase E endonucleolytic cleavages without altering cleavage site specificity or interacting detectably with substrate RNAs. Overexpression of RraA circumvents the effects of an autoregulatory mechanism that normally maintains the RNase E cellular level within a narrow range, resulting in the genome-wide accumulation of RNase E-targeted transcripts. While not required for RraA action, the C-terminal RNase E region that serves as a scaffold for formation of a multiprotein degradosome complex modulates the inhibition of RNase E catalytic activity by RraA. Our results reveal a possible mechanism for the dynamic regulation of RNA decay and processing by inhibitory RNase binding proteins. IS - 5 JF - Cell EP - 634 TI - RraA: a Protein Inhibitor of RNase E Activity that Globally Modulates RNA Abundance in E. coli VL - 114 SP - 623 KW - 1q5x KW - alphabeta KW - rnasee_inhibitor KW - s_h AU - Lee, Kangseok AU - Zhan, Xiaoming AU - Gao, Junjun AU - Qiu, Ji AU - Feng, Yanan AU - Meganathan, R AU - Cohen, Stanley AU - Georgiou, George PY - 2003/09/05/ UR - http://dx.doi.org/10.1016/j.cell.2003.08.003 ER -