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Journal of Biochemistry Advance Access originally published online on November 4, 2007
Journal of Biochemistry 2008 143(2):169-177; doi:10.1093/jb/mvm207
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© 2007 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; and 2Department of Chemistry, University of Cambridge, Lensfield Road, Cambridge CB21EW, UK

*To whom correspondence should be addressed. Tel: +48-81-5375950, Fax: +48-81-5375907, E-mail: maro{at}hektor.umcs.lublin.pl

Received August 22, 2007; Accepted October 18, 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 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.

Key Words: ribosome, ribosomal P protein, stalk

Abbreviations: CD, Circular dichroism; PBS, phosphate-buffered saline buffer; FPLC, fast protein liquid chromatography; bis-ANS - (4, 4'-dianilino-1,1'-binaphthyl-5,5'-disulfonic acid); SDS-PAGE, sodium dodecyl sulfate polyacrylamide gel electrophoresis; SEC, size-exclusion chromatography; MS, mass spectrometry


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