2mez

Flexible anchoring of archaeal MBF1 on ribosomes suggests role as recruitment factor

spinqualitylabelsall models 2mez, 16 NMR models Show:Asymmetric Unit Biological Assembly Drag the structure with the mouse to rotate   Export Animated Image   Print3D Structural highlights 2mez is a 1 chain structure. Full experimental information is available from OCA. For a guided tour on the structure components use FirstGlance. Resources: FirstGlance, OCA, RCSB, PDBsum Publication Abstract from PubMed Multi-Protein Bridging factor 1 (MBF1) is a protein containing a conserved helix-turn-helix domain in both eukaryotes and archaea. Eukaryotic MBF1 has been reported to function as a transcriptional co-activator that physically bridges transcription regulators with the core transcription initiation machinery of RNA polymerase II. In addition, MBF1 has been found to be associated with poly-adenylated mRNA in yeast as well as mammalian cells. Archaeal MBF1 (aMBF1) is very well conserved among most archaeal lineages, however, its function has remained elusive thus far. To address this we have conducted a molecular characterization of this aMBF1. Affinity purification of interacting proteins indicates that aMBF1 binds to ribosomal subunits. On sucrose density gradients, aMBF1 co-fractionates with free 30S ribosomal subunits as well as with 70S ribosomes engaged in translation. Binding of aMBF1 to ribosomes does not inhibit translation. Using NMR spectroscopy, we show that aMBF1 contains a long intrinsically disordered linker connecting the predicted N-terminal Zn-ribbon domain with the C-terminal helix-turn-helix (HTH) domain. The HTH domain, which is conserved in all archaeal and eukaryotic MBF1 homologues, is directly involved in the association of aMBF1 with ribosomes. The disordered linker of the ribosome-bound aMBF1 provides the N-terminal domain with high flexibility in the aMBF1-ribosome complex. Overall, our data suggest a role for aMBF1 in the archaeal translation process. Archaeal MBF1 binds to 30S and 70S ribosomes via its helix-turn-helix domain.,Blombach F, Launay H, Snijders AP, Zorraquino V, Wu H, de Koning B, Brouns SJ, Ettema T, Camilloni C, Cavalli A, Vendruscolo M, Dickman MJ, Cabrita LD, La Teana A, Benelli D, Londei P, Christodoulou J, van der Oost J Biochem J. 2014 May 14. PMID:24825021 From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine.

Proteopedia Page Contributors and Editors (what is this?)

OCA