This HTML5 document contains 26 embedded RDF statements represented using HTML+Microdata notation.

The embedded RDF content will be recognized by any processor of HTML5 Microdata.

Subject Item

n2:w

rdf:type

rdac:C10001 bibo:Article

dcterms:isPartOf

n18:w

dcterms:subject

n15:structuralbiology

dcterms:title

Release Factors 2 from Escherichia coli and Thermus thermophilus: structural, spectroscopic and microcalorimetric studies

rdaw:P10072

n8:web n8:print

vivo:relatedBy

n10:3 n10:6 n10:7 n10:5 n10:2 n10:8 n10:4 n10:1

marcrel:aut

n5:id n6:1c75c28caedf9b4e07b9c4ea463206b3 n2:redeckelars n2:konarevpeterv n2:zoldakgabriel n16:id n2:sedlakerik n2:voertlercstefan

dcterms:abstract

Prokaryotic class I release factors (RFs) respond to mRNA stop codons and terminate protein synthesis. They interact with the ribosomal decoding site and the peptidyl-transferase centre bridging these 75 Å distant ribosomal centres. For this an elongated RF conformation, with partially unfolded core domains II·III·IV is required, which contrasts the known compact RF crystal structures. The crystal structure of Thermus thermophilus RF2 was determined and compared with solution structure of T. thermophilus and Escherichia coli RF2 by microcalorimetry, circular dichroism spectroscopy and small angle X-ray scattering. The structure of T. thermophilus RF2 in solution at 20°C is predominantly compact like the crystal structure. Thermodynamic analysis point to an initial melting of domain I, which is independent from the melting of the core. The core domains II·III·IV melt cooperatively at the respective physiological temperatures for T. thermophilus and E. coli. Thermodynamic analyses and the X-ray scattering results for T. thermophilus RF2 in solution suggest that the compact conformation of RF2 resembles a physiological state in absence of the ribosome.

hub:articleType

n12:researcharticle

hub:isPartOfThisJournal

n17:w