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Feb 1, 2022 - Molekulaar- ja rakubioloogia andmed
Reier, Kaspar; Lahtvee, Petri-Jaan; Liiv, Aivar; Remme, Jaanus, 2022, "A conundrum of r-protein stability: unbalanced stoichiometry of r-proteins during stationary phase in Escherichia coli - Supplementary materials", https://doi.org/10.23673/RE-310, DATADOI, V1
Here we show that a specific set of r-proteins are rapidly degraded after release from the rRNA. The degradation of r-proteins is an intriguing new aspect of r-protein metabolism in bacteria. The dataset represents collection of supplementary materials used in the manuscript "A conundrum of r-protein stability: unbalanced stoichiometry of r-protein... |
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MD5: b87be18fb4408220ce1fd2d2c7cd2bde
Figure S11 – 50S subunits r-protein degradation kinetics |
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MD5: 5084440fa9102a97c5c4917987bc3490
Figure S12 – 30S subunits r-protein degradation kinetics |
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MD5: e59a8ca210319b9fc6ac08cc4a3e4fad
Figure S1 – Number of viable cells during stationary phase culture |
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MD5: 62a11643d0fef74b24c6d210a665877e
Figure S2 – Ribosome analysis of stationary phase cells using sucrose gradient centrifugation |
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Figure S3 – Presence of 100S particles in stationary phase using sucrose gradient centrifugation |
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MD5: 58cb26e8a17e12fc8b7ec5d1fe8d169a
Figure S4 – Total RNA content in cells decreases during the stationary phase |
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MD5: 106147a7b333eaf9667d1077a71e24a4
Figure S5 – 16S and 23S rRNA quantification in total RNA |
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MD5: 802f5bfc0a8562bf0ad58c58bc273c47
Figure S6 – The r-protein quantity in the 70S ribosomes does not change during the stationary phase |
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MD5: b119b620a97d911dd977d10f92ba99b1
Figure S7 – bL17 uL22 and bS6 bind non specifically to ribosomes during isolation |
