Rop protein

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Rop (also known as repressor of primer) is a small dimeric protein responsible for keeping the copy number of ColE1 family and related bacterial plasmids low in E. coli by increasing the speed of pairing between the preprimer RNA, RNA II, and its antisense RNA, RNA I. [1] Structurally, Rop is a homodimeric four-helix bundle protein formed by the antiparallel interaction of two helix-turn-helix 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.

ColE1 replication control ColE1 replication control.png
ColE1 replication control

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ColE1 is a plasmid found in bacteria. Its name derives from the fact that it carries a gene for colicin E1. It also codes for immunity from this product with the imm gene. In addition, the plasmid has a series of mobility (mob) genes. Its size and the presence of a single EcoRI recognition site caused it to be considered as a vector candidate.

In cellular biology, the plasmid copy number is the number of copies of a given plasmid in a cell. To ensure survival and thus the continued propagation of the plasmid, they must regulate their copy number. If a plasmid has too high of a copy number, they may excessively burden their host by occupying too much cellular machinery and using too much energy. On the other hand, too low of a copy number may result in the plasmid not being present in all of their host's progeny. Plasmids may be either high copy number plasmids or low copy number plasmids; the regulation mechanisms between these two types are often significantly different. Biotechnology applications may involve engineering plasmids to allow a very high copy number. For example, pBR322 is a low copy number plasmid from which several very high copy number cloning vectors have been derived.

References

  1. ^ Banner, David W.; Kokkinidis, Michael; Tsernoglou, Demetrius (August 1987). "Structure of the ColE1 Rop protein at 1.7 Å resolution". Journal of Molecular Biology. 196 (3): 657–675. doi:10.1016/0022-2836(87)90039-8. PMID   3681971.
  1. ^ Kresse, H. P.; Czubayko, M.; Nyakatura, G.; Vriend, G.; Sander, C.; Bloecker, H. (1 November 2001). "Four-helix bundle topology re-engineered: monomeric Rop protein variants with different loop arrangements". Protein Engineering Design and Selection. 14 (11): 897–901. doi: 10.1093/protein/14.11.897 . PMID   11742109.
  1. del Solar G, Espinosa M (August 2000). "Plasmid copy number control: an ever-growing story". Molecular Microbiology. 37 (3): 492–500. doi:10.1046/j.1365-2958.2000.02005.x. PMID   10931343.