RNA-Aptamers for Studying RNA Protein Interactions

Sprinzl, Mathias; Hoffmann, Hendrik; Brock, Stephan; Nanninga, Matthias; Hornung, Veronika

doi:10.1007/978-94-011-4485-8_16

Cited by 1 publication

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“…In the case of IF2 an intermolecular 'arginine finger' mechanism of GTPase activation, similar to that of Ras and rasGAP, seems to be more convincing. Sprinzl et al (1999) Brought to you by | University of California Authenticated Download Date | 6/6/15 4:02 PM…”

Section: Discussionmentioning

confidence: 99%

Regulation of GTPases in the Bacterial Translation Machinery

Sprinzl

Brock²,

Huang³

et al. 2000

Biological Chemistry

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Several GTPases participate in bacterial protein biosynthesis. Initiation factor 2 controls the formation of the ribosomal initiation complex and places initiator fMet-tRNAfMet in the ribosomal P-site. Elongation factors Tu and G are responsible for codon-specific binding of the aminoacyl-tRNA to the A-site, and peptidyl-tRNA to the P-site, respectively, during the elongation phase of protein biosynthesis. Release factor 3, a GTPase which is not ubiquitous, is involved in termination and release of the nascent polypeptide. Other translation factors, including initiation factors 1 and 3, elongation factor Ts, release factors 1 and 2, and ribosomal release factor do not belong to the family of GTP/GDP binding proteins. The guanosine nucleotide binding domains of the GTPases involved in translation are structurally related to the Galpha subunit of heterotrimeric G proteins and to the proteins of the Ras family. We have identified and sequenced all genes coding for translation factors in the extreme thermophile Thermus thermophilus. The proteins were overproduced in Escherichia coli, purified, biochemically characterised and used for crystallisation and structural analysis. Further biochemical investigations were aimed at gaining insight into the molecular mechanism underlying the regulation of the GTPase activity of the translation factors, and to elucidate the role of their ribosomal binding sites in this process.

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Section: Discussionmentioning

confidence: 99%