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Journal of Biochemistry Advance Access first published online on January 24, 2008
This version published online on January 24, 2008
Journal of Biochemistry, doi:10.1093/jb/mvn011
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© 2008 The Japanese Biochemical Society

Structural properties of the human acidic ribosomal P proteins forming the P1-P2 heterocomplex

Przemyslaw Grela1, Justyna Sawa-Makarska1, Yuliya Gordiyenko2, Carol V. Robinson2, Nikodem Grankowski1 and Marek Tchórzewski1,*

1Department of Molecular Biology, Maria Curie-Sklodowska University, Akademicka 19, 20-033 Lublin, Poland
2Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB21EW, United Kingdom

Corresponding author: *Marek Tchórzewski Department of Molecular Biology Institute of Microbiology and Biotechnology Maria Curie-Sklodowska University Akademicka 19 20-033 Lublin Poland Telephone: +48-81-5375950 Fax: +48-81-5375907 e-mail: maro{at}hektor.umcs.lublin.pl

Received November 15, 2007; Accepted November 22, 2007


  Abstract

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 divers environmental conditions. The functional differences among the P1/P2 proteins were analyzed 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.


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