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Chris Casey, Michal Harel, Jaime Prilusky, Alexander Berchansky, Joel L. Sussman

Revision as of 02:38, 14 November 2012 view source Chris Casey (talk \| contribs) 34 edits No edit summary ← Older edit		Revision as of 02:38, 14 November 2012 view source Chris Casey (talk \| contribs) 34 edits No edit summary Newer edit →
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	=== Integration of the Translocator Domain into Outer Membrane ==		== Integration of the Translocator Domain into Outer Membrane ==

	Omp85 has been found in many studies to help integrate beta barrels into the outer membrane in order to allow the autotransporter to complete its duty. Due to the <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/Hydophilic/1'>hydrophilic nature</scene>of the beta barrel’s hairpin loops on the extracellular side of NaIP, it is impossible for it to breach the cell membrane that is highly hydrophobic. Research on how this occurs in Neisseria meningitides is ongoing and has not been discovered yet. Yet there are many implications that a protein named Omp85 is most likely the helper protein that facilitates this. The large hydrophilic loops on the autotransporter domain might act as a recognition signal for the Omp85 complex to encompass the end of the beta barrel. From here the Omp85 complex which sits on the periplasmic side of the cell membrane is activated and creates a pore and places the beta barrel within the membrane, while preventing the hydrophilic loops from directly coming in contact with the hydrophobic cell membrane. Then the Omp85 molecule is able to integrate the beta barrel into the pore that it created, situating it permanently there. The lag time between Omp85 and the translocator exporting a protein is very small and it is hard to tell whether they can occur simultaneously or only occur simultaneously. <ref name="PMID: 8254661" />		Omp85 has been found in many studies to help integrate beta barrels into the outer membrane in order to allow the autotransporter to complete its duty. Due to the <scene name='Translocator_Domain_of_the_Autotransporter_NalP_within_Neisseria_meningitidis/Hydophilic/1'>hydrophilic nature</scene>of the beta barrel’s hairpin loops on the extracellular side of NaIP, it is impossible for it to breach the cell membrane that is highly hydrophobic. Research on how this occurs in Neisseria meningitides is ongoing and has not been discovered yet. Yet there are many implications that a protein named Omp85 is most likely the helper protein that facilitates this. The large hydrophilic loops on the autotransporter domain might act as a recognition signal for the Omp85 complex to encompass the end of the beta barrel. From here the Omp85 complex which sits on the periplasmic side of the cell membrane is activated and creates a pore and places the beta barrel within the membrane, while preventing the hydrophilic loops from directly coming in contact with the hydrophobic cell membrane. Then the Omp85 molecule is able to integrate the beta barrel into the pore that it created, situating it permanently there. The lag time between Omp85 and the translocator exporting a protein is very small and it is hard to tell whether they can occur simultaneously or only occur simultaneously. <ref name="PMID: 8254661" />