Quantitation of the ribosomal protein autoregulatory network using mass spectrometry.
Relative levels of ribosomal proteins were quantified in crude cell lysates using mass spectrometry. A method for quantifying cellular protein levels using macromolecular standards is presented that does not require complex sample separation, identification of high-responding peptides, affinity purification, or postgrowth modifications. Perturbations in ribosomal protein levels by overexpression of individual proteins correlate to known autoregulatory mechanisms and extend the network of ribosomal protein regulation.
Sykes
Michael T
MT
Department of Molecular Biology, The Skaggs Institute for Chemical Biology, The Scripps Research Institute, La Jolla, California 92037, USA.
Sperling
Edit
E
Chen
Stephen S
SS
Williamson
James R
JR
D004926:Escherichia coli / Q000235:genetics / Q000378:metabolism*; D029968:Escherichia coli Proteins / Q000235:genetics / Q000378:metabolism*; D015964:Gene Expression Regulation, Bacterial; D013058:Mass Spectrometry / Q000191:economics / Q000379:methods*; D016601:RNA-Binding Proteins / Q000235:genetics / Q000378:metabolism; D012269:Ribosomal Proteins / Q000235:genetics / Q000378:metabolism*
D029968:Escherichia coli Proteins; D016601:RNA-Binding Proteins; D012269:Ribosomal Proteins; C489371:rplV protein, E coli