High impact information on TOMM22

• Tom22 forms a complex with Tom20, and its cytosolic domain functions as an import receptor as in fungi [1].
• Identification and functional analysis of human Tom22 for protein import into mitochondria [1].
• We report here the identification and functional analysis of human Tom22 (hTom22). hTom22 has an N-terminal negatively charged region exposed to the cytosol, a putative transmembrane region, and a C-terminal intermembrane space region with little negative charge [1].
• Surprisingly, full-length Bbeta2 is not detectably cleaved and is retained at the outer mitochondrial membrane, even though it interacts with the TOM22 import receptor, as shown by luciferase complementation in intact cells [2].
• A mitochondrial outer membrane protein of approximately 22 kDa (1C9-2) was purified from Vero cells assessing immunoreactivity with a monoclonal antibody, and the cDNA was cloned based on the partial amino acid sequence of the trypsin-digested fragments [3].

Biological context of TOMM22

• These results indicate that the levels of Tom22 within mitochondria dictate the assembly of TOM complexes and hence may regulate its biogenesis [4].

Anatomical context of TOMM22

• The antibodies against 1C9-2 inhibited the import of a matrix-targeted preprotein into isolated mitochondria [3].

Associations of TOMM22 with chemical compounds

• This mitochondrial RNA colocalizes with components of the cytoplasmic machinery that makes and imports nuclear-encoded proteins - that is, a ribosomal protein (S6), a nascent peptide associated protein (NAC), and the translocase in the outer membrane (Tom22) [5].

Other interactions of TOMM22

• A cell-free immunoprecipitation assay indicated that an internal segment of the Tom22 cytosolic domain is important for interaction with Tom20 [1].
• One complex of approximately 400 kDa contains the receptor Tom22 and the general import pore component Tom40, the other complex of approximately 120 kDa contains the receptor Tom70 [6].

References