Protein splicing in the maturation of M. tuberculosis recA protein: a mechanism for tolerating a novel class of intervening sequence.

Abstract

The M. tuberculosis recA locus comprises an 85 kd open reading frame but produced 38 kd RecA and 47 kd products in E. coli. No RNA processing was detected; rather, an 85 kd precursor protein was spliced, releasing a 47 kd spacer protein, and joining its terminal fragments to form mature RecA protein. "Spacer" protein was also produced in M. tuberculosis and from a hybrid spacer-LacZ alpha fusion molecule. Mutagenesis at codon wobble positions at one splice junction showed that protein rather than nucleotide sequence determined splicing activity. Other mutants defined additional regions needed for splicing and allowed processing to be followed. Splicing was essential for RecA activity in E. coli. The possibility that splicing is a manifestation of a novel class of genetic element is discussed.

• Authors: E O Davis, P J Jenner, P C Brooks, M J Colston, S G Sedgwick
• Journal: Cell (Cell) Vol. 71 Issue 2 Pg. 201-10 (Oct 16 1992) ISSN: 0092-8674 [Print] United States
• PMID: 1423588 (Publication Type: Comparative Study, Journal Article)

Chemical References

• Rec A Recombinases

Topics

• Amino Acid Sequence
• Base Sequence
• Introns
• Molecular Sequence Data
• Mutagenesis, Site-Directed
• Mycobacterium tuberculosis (metabolism)
• Open Reading Frames
• Protein Processing, Post-Translational
• Rec A Recombinases (genetics, metabolism)
• Saccharomyces cerevisiae