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Comment
. 2012 May 11:2:65.
doi: 10.3389/fcimb.2012.00065. eCollection 2012.

Exoribonucleases as modulators of virulence in pathogenic bacteria

Rute G Matos  1 , Cátia Bárria, Vânia Pobre, José M Andrade, Cecília M Arraiano
Affiliations
Comment

Exoribonucleases as modulators of virulence in pathogenic bacteria

Rute G Matos et al. Front Cell Infect Microbiol. .
No abstract available

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Figures

Figure 1
Figure 1
Schematic representation of the domains found in the exoribonucleases from PNPase and RNase II families and structures of representative members. (A) Top: PNPase (PDX family) primary structure: two RNase PH catalytic domains followed by two RNA binding domains (KH and S1). PNPase is a trimer and assembles in a donut like shape (on the left; Shi et al., 2008). The S1 binding domain was shown to restore PNPase deletion effect in Yersinia (Rosenzweig et al., 2007). (B) Top: linear representation of RNase II and RNase R domains: the central catalytic RNB, and the CSD1, CSD1, and S1 RNA binding domains. Members of the family can have additional domains at the N-terminal region, namely Helix-Turn-Helix in RNase R. On the left is represented the E. coli RNase II–RNA complex crystal structure, showing the distinct domains of the enzyme, and the 13-mer bound RNA (Frazão et al., 2006). The RNB domain (in blue), is the responsible for the catalytic activity of the protein which, for example, is important for the development of competence in L. pneumophila (Charpentier et al., 2008).
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References

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    1. Andrade J. M., Pobre V., Matos A. M., Arraiano C. M. (2012). The crucial role of PNPase in the degradation of small RNAs that are not associated with Hfq. RNA 18, 844–85510.1261/rna.029413.111 - DOI - PMC - PubMed
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