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. Author manuscript; available in PMC: 2018 Jan 1.
Published in final edited form as: Subcell Biochem. 2017;84:139–160. doi: 10.1007/978-3-319-53047-5_5

Table 5.1.

Copy number of cell division and cytoskeleton proteins, determined by Li et al. (2014)

Gene MOPS complete MOPS minimal MOPS complete
Without methionine
ftsA 984 575 1013
ftsB 487 140 173
ftsE 967 320 649
ftsI 349 144 226
ftsK 508 213 376
ftsL 416 201 423
ftsN 871 269 405
ftsP 905 196 410
ftsQ 336 147 172
ftsW 293 117 169
ftsX 838 244 436
ftsZ 6750 3335 5290
zipA 2128 501 874
minC 857 364 575
minD 5358 2444 3324
minE 3597 1970 2680
matP 601 360 347
slmA 2323 568 952
zapA 2275 738 2008
zapB 34,197 7797 18,090
ZapC/YcbW 155 155 155
ZapD/YacF 1983 373 538
ZapE/YhcM 255 214 262
mreB 11,304 2393 5570
mreC 738 176 333
mreD 367 71 148
rodZ 1309 576 669

This study used ribosome profiling to determine the rate of translation of 95% of the proteins in E. coli. The rates were converted to number of protein molecules synthesized in one cell cycle. Assuming no unusual degradation, the numbers can be taken as the average number of molecules per cell. The E. coli strain MG1655 was grown at 37 °C in three different media with different doubling times: 21.5 and 56.3 min in MOPS complete and incomplete media, and 26.5 min in MOPS complete without methionine. The latter condition required the cell to substantially upregulate the met-E enzyme, altering overall metabolism. We have extracted cell division and cytoskeleton proteins from their table S1. It seems quite valuable to have these numbers determined for all proteins in the identical cell and growth conditions. The 6750 molecules of FtsZ in a cell volume of 2 × 10−15 L is 5.6 μM