Bacillus subtilis ribonucleases J1 and J2 form a complex with altered enzyme behaviour - Archive ouverte HAL Access content directly
Journal Articles Molecular Microbiology Year : 2010

Bacillus subtilis ribonucleases J1 and J2 form a complex with altered enzyme behaviour

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Agnès M Hébert
  • Function : Author
Peggy Mervelet
  • Function : Author
  • PersonId : 1206637
Lionel Benard
Audrey Dorleans
  • Function : Author
Inès Li de La Sierra-Gallay
  • Function : Author
Philippe P. Noirot
  • Function : Author
Harald Putzer
  • Function : Author
  • PersonId : 1082620
Ciarán Condon

Abstract

Ribonucleases J1 and J2 are recently discovered enzymes with dual 5'-to-3' exoribonucleolytic/endoribonucleolytic activity that plays a key role in the maturation and degradation of Bacillus subtilis RNAs. RNase J1 is essential, while its paralogue RNase J2 is not. Up to now, it had generally been assumed that the two enzymes functioned independently. Here we present evidence that RNases J1 and J2 form a complex that is likely to be the predominant form of these enzymes in wild-type cells. While both RNase J1 and the RNase J1/J2 complex have robust 5'-to-3' exoribonuclease activity in vitro, RNase J2 has at least two orders of magnitude weaker exonuclease activity, providing a possible explanation for why RNase J1 is essential. The association of the two proteins also has an effect on the endoribo-nucleolytic properties of RNases J1 and J2. While the individual enzymes have similar endonucleolytic cleavage activities and specificities, as a complex they behave synergistically to alter cleavage site preference and to increase cleavage efficiency at specific sites. These observations dramatically change our perception of how these ribonucleases function and provide an interesting example of enzyme subfunctionalization after gene duplication.

Dates and versions

hal-03347836 , version 1 (17-09-2021)

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Nathalie Mathy, Agnès M Hébert, Peggy Mervelet, Lionel Benard, Audrey Dorleans, et al.. Bacillus subtilis ribonucleases J1 and J2 form a complex with altered enzyme behaviour. Molecular Microbiology, 2010, 75 (2), pp.489-498. ⟨10.1111/j.1365-2958.2009.07004.x⟩. ⟨hal-03347836⟩
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