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Alanine scanning of MS2 coat protein reveals protein-phosphate contacts involved in thermodynamic hot spots.

Abstract：

:The co-crystal structure of the MS2 coat protein dimer with its RNA operator reveals eight amino acid side-chains contacting seven of the RNA phosphates. These eight amino acids and five nearby control positions were individually changed to an alanine residue and the binding affinities of the mutant proteins to the RNA were determined. In general, the data agreed well with the crystal structure and previous RNA modification data. Interestingly, amino acid residues that are energetically most important for complex formation cluster in the middle of the RNA binding interface, forming thermodynamic hot spots, and are surrounded by energetically less relevant amino acids. In order to evaluate whether or not a given alanine mutation causes a global change in the RNA-protein interface, the affinities of the mutant proteins to RNAs containing one of 14 backbone modifications spanning the entire interface were determined. In three of six protein mutations tested, thermodynamic coupling between the site of the mutation and RNA groups that can be even more than 16 A away was detected. This suggests that, in some cases, the mutation may subtly alter the entire protein-RNA interface.

journal_name

J Mol Biol

journal_title

Journal of molecular biology

authors

Hobson D,Uhlenbeck OC

doi

10.1016/j.jmb.2005.11.046

keywords:

subject

Has Abstract

pub_date

2006-02-24 00:00:00

pages

613-24

issue

3

eissn

0022-2836

issn

1089-8638

pii

S0022-2836(05)01444-0

journal_volume

356

pub_type

杂志文章

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