NalP: Difference between revisions

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

Revision as of 00:39, 14 November 2012 view source Chris Casey (talk \| contribs) 34 edits No edit summary ← Older edit		Revision as of 00:51, 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. Do to the hydrophilic nature of the beta barrel’s hairpin loops on the extracellular side in NaIP it is impossible for it to breach the cell membrane that is highly hydrophobic. Research of 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 auto transporter domain might act as a recognition signal for the Omp85 complex to encompass the end of the beta barrel. From here the Omp85 complex ~~transports~~ the ~~translocator toward~~ the cell membrane and ~~is able to created~~ a pore and place the beta barrel within the membrane, whilst avoiding that hydrophilic loops from directly coming in contact with the hydrophobic cell membrane. <ref name="~~NaIP~~" />		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. Do to the hydrophilic nature of the beta barrel’s hairpin loops on the extracellular side in NaIP it is impossible for it to breach the cell membrane that is highly hydrophobic. Research of 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 auto transporter 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 paraplasm side of the cell membrane is activated and creates a pore and place the beta barrel within the membrane, whilst avoiding that 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 translocater exporting a protein is very small and is hard to tell wether they can or only occur simultaneously. <ref name="PMID: 8254661" />