Structural basis of HutP-mediated anti-termination and roles of the Mg2+ ion and L-histidine ligand

Thirumananseri Kumarevel, Hiroshi Mizuno and Penmetcha K. R. Kumar ()
Additional contact information
Thirumananseri Kumarevel: Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST)
Hiroshi Mizuno: National Institute of Agrobiological Sciences
Penmetcha K. R. Kumar: Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST)

Nature, 2005, vol. 434, issue 7030, 183-191

Abstract: Abstract HutP regulates the expression of the hut structural genes of Bacillus subtilis by an anti-termination mechanism and requires two components, Mg2+ ions and l-histidine. HutP recognizes three UAG triplet units, separated by four non-conserved nucleotides on the terminator region. Here we report the 1.60-Å resolution crystal structure of the quaternary complex (HutP–l-histidine–Mg2+–21-base single-stranded RNA). In the complex, the RNA adopts a novel triangular fold on the hexameric surface of HutP, without any base-pairing, and binds to the protein mostly by specific protein–base interactions. The structure explains how the HutP and RNA interactions are regulated critically by the l-histidine and Mg2+ ion through the structural rearrangement. To gain insights into these structural rearrangements, we solved two additional crystal structures (uncomplexed HutP and HutP–l-histidine–Mg2+) that revealed the intermediate structures of HutP (before forming an active structure) and the importance of the Mg2+ ion interactions in the complexes.

Date: 2005
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature03355 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:434:y:2005:i:7030:d:10.1038_nature03355

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature03355

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().