Final answer:
An E. coli cell with a temperature-sensitive mutation in the gene for DNA ligase would likely exhibit impaired DNA replication and an accumulation of DNA breaks, aligning with option B. This is due to the crucial role of DNA ligase in joining Okazaki fragments during replication, as demonstrated through historical experiments on E. coli and T4 phage.
Step-by-step explanation:
If an E. coli cell had a temperature-sensitive mutation in the gene for DNA ligase, one would expect certain cellular properties to be affected. DNA ligase is crucial in the DNA replication process because it joins the Okazaki fragments on the lagging strand to create a continuous DNA strand. Without a functional DNA ligase, we can predict that the cell would suffer from impaired DNA replication and an accumulation of DNA breaks because the fragments generated during replication would not be efficiently joined. This leads us to anticipate that option B, which states "Impaired DNA replication; accumulation of DNA breaks," is the expected outcome of such a mutation.
Historically, experiments with E. coli and bacteriophage T4 by Reiji Okazaki and colleagues highlighted the essential role of DNA ligase in piecing together the Okazaki fragments, leading to the conclusion that a deficiency in this enzyme would lead to an accumulation of these fragments, thus slowing down the growth of T4 phage within the bacterial host.
While DNA repair efficiency may be affected as well, it does not increase; rather, the lack of DNA ligase would compromise the repair mechanism. Option A, which suggests increased efficiency and replication speed, does not align with the role of DNA ligase. Options C and D mention elevated transcription rates and enhanced translation accuracy, which are not directly related to the specific function of DNA ligase in DNA replication.