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Identification of two poly(A) polymerases in Bacillus subtilis
1Boston Biomedical Research Institute, MA 02114, USA. sarkar@bbri.harvard.edu
Biochemistry and Molecular Biology International
|April 1, 1997
Summary
Researchers found two distinct poly(A) polymerase enzymes in Bacillus subtilis, similar to those in Escherichia coli. This suggests conserved mechanisms for messenger RNA processing in both bacteria.
Area of Science:
- Molecular Biology
- Biochemistry
- Microbiology
Background:
- Polyadenylation is a crucial post-transcriptional modification of mRNA.
- Polynucleotide phosphorylase (PNPase) plays a role in RNA processing and degradation.
- Understanding poly(A) polymerase diversity is key to deciphering mRNA metabolism.
Purpose of the Study:
- To identify and characterize poly(A) polymerase activities in Bacillus subtilis.
- To compare these enzymes with those found in Escherichia coli.
- To investigate potential parallels in mRNA 3'-end processing between Gram-positive and Gram-negative bacteria.
Main Methods:
- Enzyme assays for poly(A) polymerase activity.
- Disruption of the polynucleotide phosphorylase gene in Bacillus subtilis.
- Gel filtration chromatography for molecular size determination.
Main Results:
- Two distinct poly(A) polymerase activities were detected in Bacillus subtilis extracts.
- The two enzymes differed significantly in molecular size.
- Both B. subtilis enzymes showed similarities in size and catalytic properties to E. coli poly(A) polymerases.
Conclusions:
- Bacillus subtilis possesses at least two distinct poly(A) polymerase enzymes.
- The presence of similar poly(A) polymerases in B. subtilis and E. coli indicates conserved mRNA processing pathways.
- These findings suggest common strategies for 3'-end mRNA processing in both Gram-positive and Gram-negative bacteria.