Translocase of the outer membrane

The translocase of the outer membrane (TOM) is a protein found in the outer mitochondrial membrane of the mitochondria. Its function is allow movement of proteins through this barrier and into the intermembrane space of the mitochondrion. Most of the proteins needed for mitochondrial function are encoded by the nucleus of the cell. The outer membrane of the mitochondrion is impermeable to large molecules greater than 5000 Daltons.cite book| last = Alberts| first = Bruce| authorlink = | coauthors = Alexander Johnson, Julian Lewis, Martin Raff, Keith Roberts, Peter Walter| year = 1994| title = Molecular Biology of the Cell| publisher = Garland Publishing Inc.| location = New York| isbn = 0815332181] The TOM works in conjunction with the translocase of the inner membrane (TIM) to translocate proteins into the mitochondrion. Many of the proteins in the TOM complex, such as TOMM22, were first identified in Neurospora crassa and Saccharomyces cerevisiae. [cite journal | author=Seki N, Moczko M, Nagase T, "et al." |title=A human homolog of the mitochondrial protein import receptor Mom19 can assemble with the yeast mitochondrial receptor complex. |journal=FEBS Lett. |volume=375 |issue= 3 |pages= 307–10 |year= 1996 |pmid= 7498524 |doi= ]

Protein targeting to the mitochondrion

Proteins destined for the mitochondrion have several characteristics. For example, HSP90 aids the delivery of the mitochondrial protein to the mitochondrion in an ATP-dependent process.cite journal | journal=J Biol Chem. | date=2005 Mar | volume=280 | issue=12 | pages=11535–43 | title= Dissection of the mitochondrial import and assembly pathway for human Tom40 | author=Humphries AD, Streimann IC, Stojanovski D, Johnston AJ, Yano M, Hoogenraad NJ, Ryan MT | pmid=15644312 | doi=10.1074/jbc.M413816200] The N-terminal end of the protein encodes a mitochondrial targeting sequence of 10-80 amino acids which can form amphipathic helices.cite journal | journal=Ann Rev Biochem. | volume=76 | pages=723–749 | date=2007 | doi=10.1146/annurev.biochem.76.052705.163409 | title=Translocation of Proteins into Mitochondria | author=Neupert W, Herrmann JM | pmid=17263664 ] cite journal | author=Herrmann JM, Neupert W | title=Protein transport into mitochondria | journal=Curr Opin Microbiol | volume=3 | issue=2 | date= 2000 Apr | pages=210–214 | doi=10.1016/S1369-5274(00)00077-1] Further, not all mitochondrial proteins have defined N-terminal targeting sequences. Some have "internal" sequences which lack consistent patterns.

Members of the complex

The translocase of the outer membrane (TOM) forms a complex made of Tom70, Tom22, and Tom20, along with Tom40, Tom7, Tom6, and Tom5. Tom40 is the core element of the translocase complex and Tom40 complexes with Tom22 with a mass of approximately 350k Daltons.cite journal | author=Ahting U, Thieffry M, Engelhardt H, Hegerl R, Neupert W, Nussberger S | date=2001 | journal=J. Cell Biol. | title=Tom40, the Pore-forming Component of the Protein-conducting TOM Channel in the Outer Membrane of Mitochondria | volume=153 | pages=1151–60 | doi=10.1083/jcb.153.6.1151] It forms the central protein-conducting channel with a diameter of approximately 2.5 nm. The human Tom22 is approximately 15.5k Daltons and complexes with Tom20.cite journal | journal =Mol Cell Biol. | date=2000 | volume=20 | issue=19 | pages=7205–13 | title=Identification and functional analysis of human Tom22 for protein import into mitochondria | author=Yano M, Hoogenraad N, Terada K, Mori M | pmid=10982837 | doi=10.1128/MCB.20.19.7205-7213.2000] It N-terminal end of Tom22 extends into the cytosol and is involved in preprotein binding.

References

ee also

* TOMM22