Which of the following can be a function for intrinsically disordered protein sequences?
A.High-specificity binding to other proteins
B.Cell signaling through covalent modification of the protein sequence
C.Tethering to hold interacting proteins in close proximity
D.Formation of a diffusion barrier from a dense network of such sequences
E.All of the above
You have studied mutations in a transcription regulatory protein from Bacillus subtilis
by an in vivo reporter gene assay carried out in Escherichia coli. The cis-regulatory
sequence that the protein normally recognizes was inserted upstream of a gene
encoding an enzyme that can produce a visible blue product. E. coli cells were then
transformed with the reporter construct along with the gene encoding one of the various
mutant forms of the transcription regulatory protein. Since the transcription regulatory
protein is an inhibitor, the colonies turn blue only when the mutant protein is
nonfunctional and unable to inhibit gene expression. Interestingly, you have identified a
number of “cold-sensitive” loss-of-function mutations that show the mutant phenotype
at 220C but not at 370C. Which of the following correctly describes the phenotype of
these cold-sensitive mutants?
A.Their colonies turn blue at permissive (low) temperatures.
B.Their colonies turn blue at permissive (high) temperatures.
C.Their colonies turn blue at nonpermissive (low) temperatures.
D.Their colonies turn blue at nonpermissive (high) temperatures.
What are the products of deamination of cytosine and 5-methyl cytosine, respectively?
A.Thymine and uracil
B.Thymine in both cases
C.Uracil and thymine
D.Uracil in both cases
E.Xanthine and hypoxanthine