原核生物における複製

DNA replication in prokaryotes initiates at the origin of replication, where DNA helicases unwind the double helix to create a replication fork. This unwinding exposes single-stranded DNA templates that serve as the basis for new strand synthesis. The process requires coordinated action of multiple enzymes to proceed efficiently.

Single-strand DNA binding proteins coat exposed single-stranded DNA to prevent it from re-annealing or forming secondary structures. These proteins stabilize the template strands, allowing DNA polymerase and other replication machinery to access the DNA efficiently. They remain bound until the complementary strand is synthesized.

DNA polymerase synthesizes DNA only in the 5' to 3' direction, but the two strands of the double helix run antiparallel. The leading strand is synthesized continuously toward the replication fork, while the lagging strand is synthesized discontinuously as Okazaki fragments away from the fork. This asymmetry accommodates the directional constraint of DNA polymerase.

DNA topoisomerases relieve the tension created by unwinding the double helix ahead of the replication fork. As helicases separate the strands, positive supercoiling accumulates downstream. Topoisomerases cut and rejoin DNA strands to release this tension, allowing replication to proceed without mechanical obstruction.

The replisome is a multi-protein complex that assembles at the replication fork and coordinates the activities of helicases, primase, DNA polymerase, and other enzymes. This coordinated assembly ensures efficient and accurate DNA synthesis on both strands. The replisome components and the trombone model describe how the lagging strand template loops to maintain coordination.

Prokaryotes have circular chromosomes with a single origin of replication, while eukaryotes have linear chromosomes with multiple origins. Prokaryotic replication is faster and simpler, lacking the telomere end-replication problem. Comparing mitochondrial, chloroplast, and prokaryotic genomes reveals that prokaryotic DNA replication is more similar to organellar replication than to nuclear eukaryotic replication.

Prokaryotic DNA polymerase possesses 3' to 5' exonuclease activity, allowing it to remove incorrectly paired nucleotides immediately after incorporation. This proofreading mechanism, combined with mismatch repair systems, maintains high fidelity during replication. The accuracy of base pairing and its significance in DNA replication ensures that genetic information is faithfully transmitted to daughter cells.