Final answer:
The 5' exonuclease of DNA Polymerase I can indeed remove the RNA-DNA linkage that is resistant to RNase H, which is a true statement. This activity is crucial for primer removal and gap-filling during DNA replication. Option number 1 is followed
Step-by-step explanation:
The statement that the 5' exonuclease of DNA Polymerase I can remove the RNA-DNA linkage that is resistant to RNase H is true. This enzymatic activity is responsible for removing RNA primers from the beginning (5' end) of Okazaki fragments in the lagging strand of DNA during replication. After the removal of the RNA primer by the 5' exonuclease domain, the gap is filled with DNA nucleotides by the DNA polymerase activity of the same enzyme, and subsequently, the DNA ligase seals the segments together, forming a continuous DNA strand.
DNA Polymerase I is unique in that it has this 5'→3' exonuclease activity in addition to its polymerization and proofreading functions, that are retained in the Klenow fragment after removing the exonuclease domain.