In mitochondrial protein import, TOM20 is closely associated with the pore-forming TOM40 complex and acts by recognizing and binding the N-terminal MTSs (matrix-targeting sequences), which form an amphipathicalpha helix and aid passage of the target proteins into the mitochondrial matrix.[9]
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^Goping IS, Millar DG, Shore GC (October 1995). "Identification of the human mitochondrial protein import receptor, huMas20p. Complementation of delta mas20 in yeast". FEBS Letters. 373 (1): 45–50. doi:10.1016/0014-5793(95)01010-C. PMID7589431. S2CID1204415.
^Likić VA, Perry A, Hulett J, Derby M, Traven A, Waller RF, et al. (March 2005). "Patterns that define the four domains conserved in known and novel isoforms of the protein import receptor Tom20". Journal of Molecular Biology. 347 (1): 81–93. doi:10.1016/j.jmb.2004.12.057. PMID15733919.
Schleiff E, Turnbull JL (September 1998). "Characterization of the N-terminal targeting signal binding domain of the mitochondrial outer membrane receptor, Tom20". Biochemistry. 37 (38): 13052–13058. doi:10.1021/bi980746y. PMID9748310.
Hernández JM, Giner P, Hernández-Yago J (November 1999). "Gene structure of the human mitochondrial outer membrane receptor Tom20 and evolutionary study of its family of processed pseudogenes". Gene. 239 (2): 283–291. doi:10.1016/S0378-1119(99)00409-6. PMID10548729.
Abdul KM, Terada K, Yano M, Ryan MT, Streimann I, Hoogenraad NJ, Mori M (October 2000). "Functional analysis of human metaxin in mitochondrial protein import in cultured cells and its relationship with the Tom complex". Biochemical and Biophysical Research Communications. 276 (3): 1028–1034. CiteSeerX10.1.1.379.8183. doi:10.1006/bbrc.2000.3589. PMID11027586.
Mukhopadhyay A, Avramova LV, Weiner H (April 2002). "Tom34 unlike Tom20 does not interact with the leader sequences of mitochondrial precursor proteins". Archives of Biochemistry and Biophysics. 400 (1): 97–104. doi:10.1006/abbi.2002.2777. PMID11913975.