RT Journal Article
SR Electronic
T1 Variable stoichiometry among core ribosomal proteins
JF bioRxiv
FD Cold Spring Harbor Laboratory
SP 005553
DO 10.1101/005553
A1 Nikolai Slavov
A1 Stefan Semrau
A1 Edoardo Airoldi
A1 Bogdan A. Budnik
A1 Alexander van Oudenaarden
YR 2014
UL http://biorxiv.org/content/early/2014/05/26/005553.abstract
AB Understanding the regulation and structure of the eukaryotic ribosome is essential to understanding protein synthesis and its deregulation in disease. Traditionally ribosomes are believed to have a fixed stoichiometry among their core ribosomal proteins (RPs), but recent experiments suggest a more variable composition1–6. Reconciling these views requires direct and precise quantification of RPs. We used mass-spectrometry to directly quantify RPs across monosomes and polysomes of budding yeast and mouse embryonic stem cells (ESC). Our data show that the stoichiometry among core RPs in wild-type yeast cells and ESC depends both on the growth conditions and on the number of ribosomes bound per mRNA. Furthermore, we find that the fitness of cells with a deleted RP-gene is inversely proportional to the enrichment of the corresponding RP in ribosomes bound to multiple mRNAs. Together, these findings support the existence of ribosomes with distinct protein composition and physiological function.