Structure of hibernating ribosomes studied by cryoelectron tomography in vitro and in situ.
Ribosomes arranged in pairs (100S) have been related with nutritional stress response and are believed to represent a "hibernation state." Several proteins have been identified that are associated with 100S ribosomes but their spatial organization has hitherto not been characterized. We have used cryoelectron tomography to reveal the three-dimensional configuration of 100S ribosomes isolated from starved Escherichia coli cells and we have described their mode of interaction. In situ studies with intact E. coli cells allowed us to demonstrate that 100S ribosomes do exist in vivo and represent an easily reversible state of quiescence; they readily vanish when the growth medium is replenished.
Ortiz
Julio O
JO
Department of Molecular Structural Biology, Max Planck Institute of Biochemistry, Martinsried, Germany.
Brandt
Florian
F
Matias
Valério R F
VR
Sennels
Lau
L
Rappsilber
Juri
J
Scheres
Sjors H W
SH
Eibauer
Matthias
M
Hartl
F Ulrich
FU
Baumeister
Wolfgang
W
D020285:Cryoelectron Microscopy / Q000379:methods*; D004926:Escherichia coli / Q000166:cytology / Q000378:metabolism; D029968:Escherichia coli Proteins / Q000032:analysis; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D011487:Protein Conformation; D012269:Ribosomal Proteins / Q000032:analysis; D012270:Ribosomes / Q000737:chemistry* / Q000378:metabolism; D014054:Tomography / Q000379:methods*
D029968:Escherichia coli Proteins; D012269:Ribosomal Proteins