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

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...

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Published in:Journal of biochemistry (Tokyo) 2008-02, Vol.143 (2), p.169-177
Main Authors: Grela, Przemysław, Sawa-Makarska, Justyna, Gordiyenko, Yuliya, Robinson, Carol V, Grankowski, Nikodem, Tchórzewski, Marek
Format: Article
Language:English
Subjects:
Chromatography, Gel
Electrophoresis, Polyacrylamide Gel
Humans
Mass Spectrometry
Protein Conformation
ribosomal P protein
Ribosomal Proteins - chemistry
ribosome
Spectrometry, Fluorescence
stalk
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Summary: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.
ISSN:0021-924X
1756-2651
DOI:10.1093/jb/mvm207