Read the passage.
Researchers studying bacteria from Antarctic sea ice have discovered several enzymes that remain active at temperatures close to 0 °C. These cold-adapted enzymes allow the bacteria to carry out essential metabolic reactions even in extremely cold conditions. One such enzyme, called lipase-A, helps the bacteria break down lipids for energy. Compared to similar enzymes from bacteria in warmer environments, lipase-A is made up of a slightly different strcuture, giving it a more flexible structure. This flexibility appears to allow it to function efficiently at lower temperatures. Scientists sequenced the gene for lipase-A and compared it to the version found in a closely related species that lives in temperate waters. The coding region for lipase-A in the Antarctic bacteria contained several base substitutions. However, the amino acid sequence was still very similar between the two species, suggesting that many of the mutations were neutral. To study how the enzyme is produced, researchers isolated the mRNA for lipase-A. They then inserted the gene into bacterial cells to produce large amounts of the lipase enzyme in the laboratory. |
Name the monomer(s) that lipase-A will break down the bacterial lipid molecules into. (Paragraph 2)
(i) Suggest one advantage to the Antarctic bacteria of having enzymes that can function at low temperatures. (Paragraph 2)
(ii) The amino acid sequence of lipase-A in cold-climate bacteria is very similar to that of the temperate bacteria, despite DNA differences. (Paragraph 3)
Explain how this is possible.
Before the researchers isolated the mRNA for lipase-A, it was produced from a gene.
(i) Describe how this mRNA was made.(Paragraph 4)
(ii) Give two ways in which the structure of this mRNA differs from the DNA it was transcribed from.
The researchers described some of the base substitutions as “neutral.” (Paragraph 3)
Describe what is meant by a neutral mutation.
Did this page help you?