B30.2/SPRY domain in tripartite motif-containing 22 is essential for the formation of distinct nuclear bodies.
Tripartite motif-containing 22 (TRIM22) is an important antiviral protein that forms distinct nuclear bodies (NB) in many cell types. This study aims to identify functional domains/residues for TRIM22's nuclear localization and NB formation. Deletion of the really-interesting-new-gene (RING) domain, which is essential for its antiviral property, abolished TRIM22 NB formation. However, mutation of two critical residues Cys15 and Cys18 to alanine in the RING domain, did not affect NB formation notably. Although the deletion of the putative bipartite nuclear localization signal (NLS) abolished TRIM22 localization and NB formation, the B30.2/SplA and ryanodine receptor (SPRY) domain, and residues 491-494 specifically are also essential for nuclear localization and NB formation.
Sivaramakrishnan
Gayathri
G
School of Biological Sciences, Nanyang Technological University, Singapore, Singapore.
Sun
Yang
Y
Rajmohan
Rajamuthiah
R
Lin
Valerie C L
VC
D000595:Amino Acid Sequence; D002460:Cell Line; D002467:Cell Nucleus / Q000378:metabolism / Q000648:ultrastructure; D003545:Cysteine / Q000737:chemistry; D006801:Humans; D015778:Minor Histocompatibility Antigens; D008969:Molecular Sequence Data; D016297:Mutagenesis, Site-Directed; D019913:Nuclear Localization Signals / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D017434:Protein Structure, Tertiary; D011994:Recombinant Proteins / Q000737:chemistry / Q000235:genetics / Q000378:metabolism; D012097:Repressor Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism*; D017384:Sequence Deletion; D014162:Transfection; D000070584:Tripartite Motif Proteins
D015778:Minor Histocompatibility Antigens; D019913:Nuclear Localization Signals; D011994:Recombinant Proteins; D012097:Repressor Proteins; C094314:TRIM22 protein, human; D000070584:Tripartite Motif Proteins; D003545:Cysteine