Difference between revisions of "Part:BBa K2259010"

(Usage in SynORI system)
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Rop dimer is a bundle of four tightly packed alpha helices that are held by hydrophobic interactions (Fig. 1).
 
Rop dimer is a bundle of four tightly packed alpha helices that are held by hydrophobic interactions (Fig. 1).
  
==Usage in SynORI system==
+
==Usage with SynORI (Framework for multi-plasmid systems)==
  
 
===Characterization of Rop protein (Vilnius-Lithuania 2017)===
 
===Characterization of Rop protein (Vilnius-Lithuania 2017)===
 
  
 
==References==
 
==References==
 
<references />
 
<references />

Revision as of 23:24, 18 October 2017


Rop protein - global copy number inhibitor (SynORI framework)

Rop (also known as repressor of primer) is a small protein responsible for keeping the copy number of ColE1 and related bacterial plasmids low in E. coli. Inhibits plasmid replication of all SynORI framework plasmid groups non-specifically, also other ColE1 replicon plasmids.



Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]


Formatting test Figure 1: Plasmid map of the plasmid p68 used for the characterization of PalcA.

Introduction

Biology

Repressor of primer (ROP) is a small dimeric protein that participates in ColE1 plasmid family copy number contro, by increasing affinity between two complementary RNAs - RNA I (Replication inhibitor) and RNA II (Replication activator). [1] By increasing affinity of the two RNA molecules Rop decreases the rate of of plasmid replication initiation events.

Rop dimer is a bundle of four tightly packed alpha helices that are held by hydrophobic interactions (Fig. 1).

Usage with SynORI (Framework for multi-plasmid systems)

Characterization of Rop protein (Vilnius-Lithuania 2017)

References

  1. Castagnoli L, Scarpa M, Kokkinidis M, Banner DW, Tsernoglou D, Cesareni G. Genetic and structural analysis of the ColE1 Rop (Rom) protein. The EMBO Journal. 1989;8(2):621-629.