Difference between revisions of "Part:BBa K676011"

Revision as of 04:20, 22 September 2011

Gyrase Binding Site from pSC101

The gyrase site cloned from pSC101 plasmid.

The pSC101 GBS (highly efficient binding and yet lack of stimulation of supercoiling) from Oram (2003) raise the possibility that the biological effects of gyrase at par are purely structural, for example , local changes in DNA topology due to the wrapping of DNA by gyrase may be already enough to induce the downstream effects of gyrase on pSC101 replication and partition.

Subsequent studies concluded that the key function of par was to cause a local increase in superhelical density in the origin region of pSC101 (Conley and Cohen, 1995), this in turn was critical in determining the interactions of other replication and partition proteins with the origin itself (Miller and Cohen,1999).However ,further experiments will be necessary to address specific questions relating to the role of gyrase function at par at a more detailed or molecular level.

From the studies, it was also found that the pSC101 GBS was cleaved by gyrase much more efficiently than pBR322 site, but plasmid with pBR322 GBS was supercoiled much better than the one with pSC101. But still the best supercoiling efficiency was achieved by the plasmid with Mu GBS

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]

@@ Line 4: / Line 4: @@
 The gyrase site cloned from pSC101 plasmid.
-<!-- Add more about the biology of this part here
-===Usage and Biology===
 The pSC101 GBS (highly efficient binding and yet lack of stimulation of
 supercoiling) from  Oram (2003)  raise the possibility that the biological effects of gyrase at par are purely structural, for example , local changes in DNA topology due to the wrapping of DNA by gyrase may be already enough to induce the downstream effects of gyrase on pSC101 replication and partition.
@@ Line 14: / Line 12: @@
 From the studies, it was also found that  the pSC101 GBS was cleaved  by gyrase much more efficiently than pBR322 site, but plasmid with pBR322 GBS  was supercoiled much better than the one with pSC101. But still the best supercoiling efficiency was achieved by the plasmid with Mu GBS
+<!-- The pSC101 GBS (highly efficient binding and yet lack of stimulation of
+supercoiling) from  Oram (2003)  raise the possibility that the biological effects of gyrase at par are purely structural, for example , local changes in DNA topology due to the wrapping of DNA by gyrase may be already enough to induce the downstream effects of gyrase on pSC101 replication and partition.
+Subsequent studies concluded that the key function of par was to cause a local increase in
+superhelical density in the origin region of pSC101 (Conley and Cohen, 1995), this in turn was critical in
+determining the interactions of other replication and partition proteins with the origin itself (Miller and Cohen,1999).However ,further experiments will be necessary to address specific questions relating to the role of gyrase function at par at a more detailed or molecular level.
+From the studies, it was also found that  the pSC101 GBS was cleaved  by gyrase much more efficiently than pBR322 site, but plasmid with pBR322 GBS  was supercoiled much better than the one with pSC101. But still the best supercoiling efficiency was achieved by the plasmid with Mu GBS
+===Usage and Biology===
 <!-- -->