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Rop (also known as repressor of primer, or as RNA one modulator (ROM)) is a small dimeric protein responsible for keeping the copy number of ColE1 family and related bacterial
plasmids A plasmid is a small, extrachromosomal DNA molecule within a cell that is physically separated from chromosomal DNA and can replicate independently. They are most commonly found as small circular, double-stranded DNA molecules in bacteria; howev ...
low in '' E. coli'' by increasing the speed of pairing between the preprimer RNA, RNA II, and its
antisense RNA Antisense RNA (asRNA), also referred to as antisense transcript, natural antisense transcript (NAT) or antisense oligonucleotide, is a single stranded RNA that is complementary to a protein coding messenger RNA (mRNA) with which it hybridizes, an ...
, RNA I. Structurally, Rop is a homodimeric four-helix bundle protein formed by the antiparallel interaction of two
helix-turn-helix Helix-turn-helix is a DNA-binding protein (DBP). The helix-turn-helix (HTH) is a major structural motif capable of binding DNA. Each monomer incorporates two α helices, joined by a short strand of amino acids, that bind to the major groove o ...
monomers. The Rop protein's structure has been solved to high resolution. Due to its small size and known structure, Rop has been used in protein design work to rearrange its helical topology and reengineer its loop regions. In general, the four-helix bundle has been extensively used in de novo protein design work as a simple model to understand the relationship between amino acid sequence and structure.


External links


Rop protein
from Proteopedia


References

{{protein-stub Proteins