Different subcellular localisations of TRIM22 suggest species-specific function.
The B30.2/SPRY domain is present in many proteins, including various members of the tripartite motif (TRIM) protein family such as TRIM5alpha, which mediates innate intracellular resistance to retroviruses in several primate species. This resistance is dependent on the integrity of the B30.2 domain that evolves rapidly in primates and exhibits species-specific anti-viral activity. TRIM22 is another positively selected TRIM gene. Particularly, the B30.2 domain shows rapid evolution in the primate lineage and recently published data indicate an anti-viral function of TRIM22. We show here that human and rhesus TRIM22 localise to different subcellular compartments and that this difference can be assigned to the positively selected B30.2 domain. Moreover, we could demonstrate that amino acid changes in two variable loops (VL1 and VL3) are responsible for the different subcellular localisations.
Herr
Anna-Maria
AM
Department of Primate Genetics, German Primate Center, Göttingen, Germany. aherr@gwdg.de
Dressel
Ralf
R
Walter
Lutz
L
D000595:Amino Acid Sequence; D000818:Animals; D049452:Green Fluorescent Proteins / Q000235:genetics; D006801:Humans; D008253:Macaca mulatta; D015778:Minor Histocompatibility Antigens; D008958:Models, Molecular; D008969:Molecular Sequence Data; D017434:Protein Structure, Tertiary; D012097:Repressor Proteins / Q000032:analysis* / Q000737:chemistry; D013045:Species Specificity; D000070584:Tripartite Motif Proteins
D015778:Minor Histocompatibility Antigens; D012097:Repressor Proteins; C094314:TRIM22 protein, human; D000070584:Tripartite Motif Proteins; D049452:Green Fluorescent Proteins