We report the structural and biophysical consequences of cysteine substitutions in the DNA-binding replication terminator protein (RTP) of Bacillus subtilis, that resulted in an optimised RTP mutant suitable for structural studies.
Together with previous data showing presence of DinoSL in transcripts of form II Rubisco and single-stranded DNA-binding replication protein A [1], the two other genes also suspected to lack SL [7], we demonstrated the presence of DinoSL in the transcripts of all the twelve genes, thereby reinstating the postulation that DinoSL occurs widely in dinoflagellate nuclear-encoded transcripts.
In this case, recruitment of Rad18 by the ssDNA-binding replication protein A (RPA) was found to be required for ubiquitylation in vivo (Davies et al, 2008).
These foci are thought to correspond to Rad51 containing nucleoprotein filaments in the Dsb recombination process (Haaf et al, 1995; Yamamoto et al, 1996) and contain the ssDNA-binding replication protein A (RPA), Rad52 and Rad54 (Golub et al, 1998; Gupta et al, 1998; Liu et al, 1999; Tan et al, 1999).
If K36me1 and –me3 have opposite effects on Cdc45 binding to replication origins, they may have opposite dynamics during DNA replication.
In this model the single-stranded DNA binding protein replication protein-A (RPA) might bind to the 5' ends and recruit the endonucleases Dna2 or Fen1 and the exonuclease Exo1 to cleave the RNA primer at the 5' end of plus strands (Figure 4, [24], [25]).
Deletion of SET2 delays Cdc45 binding to replication origins, suggesting a positive function of H3 K36 methylation in replication initiation.
The deletion of DS results in a loss of oriP-specific binding of replication initiation proteins, which leads to an increased loss of replication competence in case of very small plasmids, but is tolerated in case of large EBV genomes [14], [15].
The RFA1 gene encodes the large subunit of the yeast trimeric single-stranded DNA binding protein replication protein A (RPA), which is known to play a critical role in DNA replication.
Together with CTIP, the MRN complex promotes resection of DSB ends to produce single-stranded DNA (ssDNA) overhangs that are protected from forming secondary structures or from nuclease degradation by binding of replication protein A (RPA).
A pair of positively charged residues within the amphipathic helix (the basic amino acid PI 4,5 P2 pincer domain) was required for PI 4,5 P2 binding and replication of the HCV-RNA genome.
