Publications by authors named "D H Bechhofer"
Article Synopsis
- The study focuses on Escherichia coli's YicC protein, a newly identified ribonuclease crucial for RNA processing in living organisms.
- Researchers have characterized the structure of YicC in two forms: an unbound state (apo) and one bound to RNA, revealing unique structural features like a clamshell shape that are different from known ribonucleases.
- Findings highlight the importance of a specific domain (DUF1732) in RNA binding and catalytic activity, providing new insights into the functions of the YicC RNase family.
Article Synopsis
- RNA processing is essential for regulating functions in all living organisms.
- A new family of endoribonucleases, which are enzymes that cut RNA, has been found in bacteria and is structurally conserved.
- The study reveals that the enzyme YicC forms a hexameric channel that interacts with RNA, specifically cleaving a hairpin structure to produce shorter RNA fragments.
All cells employ a combination of endo- and exoribonucleases to degrade long RNA polymers to fragments 2-5 nucleotides in length. These short RNA fragments are processed to monoribonucleotides by nanoRNases. Genetic depletion of nanoRNases has been shown to increase abundance of short RNAs.
View Article and Find Full Text PDFThe Bacillus subtilis genome encodes four 3' exoribonucleases: polynucleotide phosphorylase (PNPase), RNase R, RNase PH, and YhaM. Previous work showed that PNPase, encoded by the gene, is the major 3' exonuclease involved in mRNA turnover; in a deletion strain, numerous mRNA decay intermediates accumulate. Whether B.
View Article and Find Full Text PDFThe genome is predicted to encode numerous ribonucleases, including four 3' exoribonucleases that have been characterized to some extent. A strain containing gene knockouts of all four known 3' exoribonucleases is viable, suggesting that one or more additional RNases remain to be discovered. A protein extract from the quadruple RNase mutant strain was fractionated and RNase activity was followed, resulting in the identification of an enzyme activity catalyzed by the YloC protein.
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