Biology:Ter protein
| Ter | |||||||||
|---|---|---|---|---|---|---|---|---|---|
 Nmr study of the proline repeat from tus | |||||||||
| Identifiers | |||||||||
| Symbol | Ter | ||||||||
| Pfam | PF05472 | ||||||||
| InterPro | IPR008865 | ||||||||
| SCOP2 | 5eau / SCOPe / SUPFAM | ||||||||
| |||||||||
In molecular biology, the Ter protein, also known as, DNA replication terminus site-binding protein, refers to a protein domain which binds to the DNA replication terminus site. Ter proteins are found in some bacterial species. They are required for the termination of DNA replication and function by binding to DNA replication terminator sequences, thus preventing the passage of replication forks.[1] The termination efficiency is affected by the affinity of a particular protein for the terminator sequence.
Function
A DNA replication terminus (ter) has a role in preventing progress of the DNA replication fork.[2] Therefore, a DNA replication terminus site-binding protein binds to this site helping to block the DNA replication fork. There are two genes controlling ter-binding activity, named tau and tus.[1]
Protein domains
The Ter protein contains two domains. The N-terminal domain is composed of an alpha helices, beta sandwich, and three loops. The C-terminal domain is made of two alpha helices and one beta sheet.[3]
References
- ↑ 1.0 1.1 "Purification of a DNA replication terminus (ter) site-binding protein in Escherichia coli and identification of the structural gene". J. Biol. Chem. 264 (35): 21031–7. December 1989. PMID 2687269.
- ↑ "A newly identified DNA replication terminus site, TerE, on the Escherichia coli chromosome.". J Bacteriol 173 (1): 391–3. 1991. PMID 1824765.
- ↑ "Structure of a replication-terminator protein complexed with DNA.". Nature 383 (6601): 598–603. 1996. doi:10.1038/383598a0. PMID 8857533. https://www.ncbi.nlm.nih.gov/entrez/eutils/elink.fcgi?dbfrom=pubmed&tool=sumsearch.org/cite&retmode=ref&cmd=prlinks&id=8857533.
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