Journal Article

Structural Properties of the Human Acidic Ribosomal P Proteins Forming the P1–P2 Heterocomplex

Przemysław Grela, Justyna Sawa-Makarska, Yuliya Gordiyenko, Carol V. Robinson, Nikodem Grankowski and Marek Tchórzewski

in The Journal of Biochemistry

Published on behalf of The Japanese Biochemical Society

Volume 143, issue 2, pages 169-177
Published in print February 2008 | ISSN: 0021-924X
Published online November 2007 | e-ISSN: 1756-2651 | DOI: http://dx.doi.org/10.1093/jb/mvm207
Structural Properties of the Human Acidic Ribosomal P Proteins Forming the P1–P2 Heterocomplex

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The ribosome has a morphologically distinct structural feature called the stalk, recognized as a vital element for its function. The ribosomal P proteins constitute the main part of the eukaryotic ribosomal stalk, forming a pentameric structure P0–(P1–P2)2. The group of P1/P2 proteins in eukaryotes is very diverse, and in spite of functional and structural similarities they do not fully complement one another, probably constituting an adaptive feature of the ribosome from a particular species to diverse environmental conditions. The functional differences among the P1/P2 proteins were analysed in vivo several times; however, a thorough molecular characterization was only done for the yeast P1/P2 proteins. Here, we report a biophysical analysis of the human P1 and P2 proteins, applying mass spectrometry, CD and fluorescence spectroscopy, cross-linking and size exclusion chromatography. The human P1/P2 proteins form stable heterodimer, as it is the case for P1/P2 from yeast. However, unlike the yeast complex P1A–P2B, the human P1–P2 dimer showed a three-state transition mechanism, suggesting that an intermediate species may exist in solution.

Keywords: ribosome; ribosomal P protein; stalk

Journal Article.  5443 words.  Illustrated.

Subjects: Biochemistry

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