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B30.2/SPRY domain in tripartite motif‐containing 22 is essential for the formation of distinct nuclear bodies
Author(s) -
Sivaramakrishnan Gayathri,
Sun Yang,
Rajmohan Rajamuthiah,
Lin Valerie C.L.
Publication year - 2009
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2009.05.036
Subject(s) - nuclear localization sequence , nls , ring finger , nuclear transport , chemistry , microbiology and biotechnology , nuclear protein , biology , cell nucleus , gene , biochemistry , transcription factor , nucleus
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.