1. (a) Cells will express β-galactosidase, lac permease, and thiogalactoside transacetylase even in the absence of lactose. (b) Cells will express β-galactosidase, lac permease, and thiogalactoside transacetylase even in the absence of lactose. (c) The levels of catabolic enzymes such as β-galactosidase and arabinose isomerase will remain low even at low levels of glucose.
2. The concentration is 1/(6 × 1023) moles per 10−15 liter = 1.7 = 10−9 M. Because Kd = 10−13 M, the single molecule should be bound to its specific binding site.
3. The number of possible 8-
4. The lac repressor does not bind DNA when the repressor is bound to a small molecule (the inducer), whereas the pur repressor binds DNA only when the repressor is bound to a small molecule (the corepressor). The E. coli genome contains only a single lac repressor-
A45
5. Anti-
6. The inverted repeat may be a binding site for a dimeric DNA-
7. Bacteriophage λ would be more likely to enter the lytic phase because the cooperative binding of the λ repressor to OR2 and OR1, which supports the lysogenic pathway, would be disrupted.
8.
λ repressor gene |
−10 region |
GATTTA |
−35 region |
TAGATA |
Cro gene |
−10 region |
TAATGG |
−35 region |
TTGACT |
There are four differences in the −10 region and three differences in the −35 region.
9. Increased Cro concentration reduces the expression of the λ repressor gene. Increased λ repressor concentration reduces the expression of the Cro gene. At low λ repressor concentrations, increased λ repressor concentration increases the expression of the λ repressor gene. At higher λ repressor concentrations, increased λ repressor concentration decreases the expression of the λ repressor gene.
10. Normally, bacterial mRNAs have a leader sequence in which a Shine–
11. Add each compound to a culture of V. fischeri at low density and look for the development of luminescence.
12. ACC, 7; ACA, 1; ACU, 0; ACG, 0.
13. Retention. The reaction likely proceeds in two steps: Attack of Glu 537 on the carbon of the galactose moiety (with inversion) followed by attack of water on this carbon (with a second inversion) to release the galactose from the enzyme.
14. The footprint appears to have approximately 50% of its intensity near 3.7 nM so that the dissociation constant is approximately 3.7 nM, corresponding to a standard free energy of binding of −48 kJ/mol (−11 kcal/mol) at T = 298K.