YxiN is a modular protein combining a DEx(D/H) core and a specific RNA-binding domain. Journal Article uri icon



  • DEx(D/H) proteins, typically described as RNA helicases, participate in rearrangement of RNA-RNA and possibly RNA-protein complexes in the cell. Aside from the conserved DEx(D/H) core, members of this protein family often contain N- and C-terminal extensions that are responsible for additional functions. The Bacillus subtilis DEx(D/H)-box protein YxiN and its Escherichia coli ortholog DbpA contain an approximately 80 amino acid C-terminal extension that has been proposed to specifically interact with a region of 23 S ribosomal RNA including hairpin 92. In this study, the DEx(D/H)-box core and the C-terminal domain of YxiN were expressed and characterized as separate proteins. The isolated DEx(D/H)-box core, YxCat, had weak, nonspecific RNA binding activity and showed RNA-stimulated ATPase activity with a Km(ATP) that resembled several non-specific DEx(D/H) proteins. The isolated C-terminal domain, YxRBD, bound RNA with the high affinity and specificity seen with full-length YxiN. Thus, YxiN is a modular protein combining the activities of the YxCat and YxRBD domains. Footprinting of YxiN and YxRBD on a 172-nucleotide fragment of 23 S rRNA was used to identify the sites of interaction of the C-terminal and helicase domains with the RNA.

publication date

  • October 21, 2005

has subject area

has restriction

  • hybrid

Date in CU Experts

  • October 18, 2013 3:36 AM

Full Author List

  • Karginov FV; Caruthers JM; Hu Y; McKay DB; Uhlenbeck OC

author count

  • 5

Other Profiles

International Standard Serial Number (ISSN)

  • 0021-9258

Additional Document Info

start page

  • 35499

end page

  • 35505


  • 280


  • 42