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Replication forks proceed from the origin of the circular chromosome in opposite directions, creating a characteristic theta structure . Although the use of two active polymerase complexes is clearly faster than one, this mechanism generates difficulty when it comes to terminating replication. Among other factors, the presence of DNA-associated proteins causes the two replication complexes to proceed at different rates, and they therefore do not necessarily meet directly opposite the origin. However, the position of termination is not random, and is defined by the presence of termination sites which associate protein factors capable of halting the advance of the replication fork from only one direction. From their positions within the chromosome and their directionality, you can see that this occurs only once the complex has traversed more than half of the total DNA.
Replication forks proceed from the origin of the circular chromosome in opposite directions, creating a characteristic theta structure . Although the use of two active polymerase complexes is clearly faster than one, this mechanism generates difficulty when it comes to terminating replication. Among other factors, the presence of DNA-associated proteins causes the two replication complexes to proceed at different rates, and they therefore do not necessarily meet directly opposite the origin. However, the position of termination is not random, and is defined by the presence of termination sites which associate protein factors capable of halting the advance of the replication fork from only one direction. From their positions within the chromosome and their directionality, you can see that this occurs only once the complex has traversed more than half of the total DNA.
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=The Proteins=
=The Proteins=
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<Structure load='2EFW' size='300' frame='true' align='right' caption='RTP' scene='Sandbox20/2efw/3' />
<Structure load='2EFW' size='300' frame='true' align='right' caption='RTP' scene='Sandbox20/2efw/3' />


This is the area for text about RTP
This is the area for text about RTP.
 
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===Tus===
===Tus===
<Structure load='2EWJ' size='300' frame='true' align='right' caption='Tus' scene='Sandbox20/Tus/2' />
<Structure load='2EWJ' size='300' frame='true' align='right' caption='Tus' scene='Sandbox20/Tus/2' />


This is the area for text about Tus
This is the area for text about Tus. Original picture is <scene name='Sandbox20/Tus/2'>shown by clicking here</scene>.


Tus binds to a conserved cytosine residue which is not base paired. The interactions between residues of the Tus protein and this unpaired cytosine nucleotide are <scene name='Sandbox20/Tus/9'>shown by clicking here</scene>.
Tus binds to a conserved cytosine residue which is not base paired <scene name='Sandbox20/Tus/13'>as shown by clicking here</scene>. The interactions between residues of the Tus protein and this unpaired cytosine nucleotide are <scene name='Sandbox20/Tus/9'>shown by clicking here</scene>.

Revision as of 04:50, 28 April 2011

IntroductionIntroduction

Replication Termination in E. coli and B. subtilisReplication Termination in E. coli and B. subtilis

Schematic representation of the replication termination fork and fork traps of the E. coli and B. subtilis chromosomes.

Replication forks proceed from the origin of the circular chromosome in opposite directions, creating a characteristic theta structure . Although the use of two active polymerase complexes is clearly faster than one, this mechanism generates difficulty when it comes to terminating replication. Among other factors, the presence of DNA-associated proteins causes the two replication complexes to proceed at different rates, and they therefore do not necessarily meet directly opposite the origin. However, the position of termination is not random, and is defined by the presence of termination sites which associate protein factors capable of halting the advance of the replication fork from only one direction. From their positions within the chromosome and their directionality, you can see that this occurs only once the complex has traversed more than half of the total DNA.

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The ProteinsThe Proteins

RTPRTP

RTP

Drag the structure with the mouse to rotate

This is the area for text about RTP.

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TusTus

Tus

Drag the structure with the mouse to rotate

This is the area for text about Tus. Original picture is .

Tus binds to a conserved cytosine residue which is not base paired . The interactions between residues of the Tus protein and this unpaired cytosine nucleotide are .

Proteopedia Page Contributors and Editors (what is this?)Proteopedia Page Contributors and Editors (what is this?)

Student, Craig T Martin, Michael Webster