(in such case, it is expected that rpoS mutants outcompete the wild type cells.)

In such case, it would be more advantageous to use up all the nutrients and the rpoS mutants may be more fit than the wild type cells.

Obviously, conserving the limiting nutrients by the wild type cells is one form of cooperation and rpoS mutants may appear as cheaters.

1) for the wild type cells in the following way.

To quantitatively analyze the survival kinetics of the wild type cells under starvation, we re-plotted the data in a manner that reveals the power law exponent of exponential functions; we denoted the number of colony-forming units at the time zero by NO and plotted log (N0 /NCFU) against time in a log-log plot (Fig.

This is higher than that of the wild type strain, —/,4 0 (= —0.018 hr '1), consistent with previous observation [18,25].

However, the period is much shorter than the period of gradual decay for the wild type cells (green region); note that the exact determination of this period is discussed below and in Fig.

This indicates that rpoS plays an important role for the wild type strain to maintain

Note that at intermediate substrate concentrations, A of ArpoS strain is higher than that of the wild type strain [30—32].

Also, note that when the substrate is completely exhausted, the culture of the ArpoS strain loses viability more rapidly than the wild type strain (see [18,25] and Fig.

28); thus, the value of A(0) of ArpoS strain should be less than that of the wild type strain.

In particular, the stability of the quintuple mutant (T68N,Q108D,T113V,E120P,S138Y) was found to be substantially higher than that of the wild type protein (Table 1), with Tm 7.2°C higher than WT, and Cm, the urea concentration at the mid-unfolding point, was 0.43M higher than WT.

A single colony of the transformed E. coli carrying the wild type or mutation dhfr was cultured in Luria-Bertani liquid medium containing 50 ug/mL kanamycin (LB-kana) at 30°C overnight, and then inoculated to fresh LB-kana (1:100 dilution) and incubated again at 30°C.

The wild type dhfr gene was cloned in a pET24 expression vector under the inducible T7 promoter, then transformed into BL21(DE3) cells [69].

The RMSDs of DHFR wild type and mutants 11 15A and 1155T vs. Monte Carlo step at temperatures from 0.1 to 3.2.

The total energy of DHFR wild type and mutants 11 15A and 1155T vs. Monte Carlo step at temperatures from 0.1 to 3.2.

The number of contacts for DHFR wild type and mutants 11 15A and 1155T vs.

(A) Correlation between simulated Tm and experimental Tm, averaging over different numbers of replications, for the DHFR wild type and mutants.

(B) Correlation between the simulated Tm and experimental Tm with different numbers of MC steps and 50 replications, forthe DHFR wild type and mutants.

The requirement to enter mitosis here equals the one in the wild type so that, in Model-1, CLN overexpressing cells are very similar in size compared with wild type cells.

Shown are culture averages of G1 and S-Gz-M durations, and the average volume at birth, at START and at budding for fast growing Wild type (WT, solid empty bars) and CLN over producing (oCLN, dashed empty bars) cells.

(A) Cell size distributions are shown for the fast growing wild type (WT, solid lines) and CLN over producing mutant (OE-CLN, dashed lines) simulated with Model-1 (red) and Model-2 (blue), corresponding to a CLN3 overexpression mutant in vivo.

(B) Average length of G1, S-GZ-M and average cell volume are shown for the wild type (solid bars) and OE-CLN cells (dashed bars) simulated with Model-1 (red) and Model-2 (blue).