Abstract:
:We present the results of in vitro binding studies aimed at defining the key recognition elements on the MS2 RNA translational operator (TR) essential for complex formation with coat protein. We have used chemically synthesized operators carrying modified functional groups at defined nucleotide positions, which are essential for recognition by the phage coat protein. These experiments have been complemented with modification-binding interference assays. The results confirm that the complexes which form between TR and RNA-free phage capsids, the X-ray structure of which has recently been reported at 3.0 A, are identical to those which form in solution between TR and a single coat protein dimer. There are also effects on operator affinity which cannot be explained simply by the alteration of direct RNA-protein contacts and may reflect changes in the conformational equilibrium of the unliganded operator. The results also provide support for the approach of using modified oligoribonucleotides to investigate the details of RNA-ligand interactions.
journal_name
Nucleic Acids Resjournal_title
Nucleic acids researchauthors
Stockley PG,Stonehouse NJ,Murray JB,Goodman ST,Talbot SJ,Adams CJ,Liljas L,Valegård Kdoi
10.1093/nar/23.13.2512subject
Has Abstractpub_date
1995-07-11 00:00:00pages
2512-8issue
13eissn
0305-1048issn
1362-4962pii
5w0036journal_volume
23pub_type
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