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Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit.
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HIV-1 Gag NC domain interacts with the ribosomal protein RPL7 endowed with nucleic acid chaperone activity, favoring the notion that RPL7 could be a Gag helper chaperoning factor possibly contributing to the start of Gag assembly
In case of L7, importin beta2 or importin beta3 are preferentially used by clusters with a high import efficiency.
RPL7 gene expression is decreased in follicular variant of papillary thyroid carcinoma.
importin beta3 is essential for the nuclear import of RPL7. The import is mediated via the multifaceted basic amino acid clusters present in the NH(2)-region of RPL7, and is RanGTP-dependent
Ribosomes, the organelles that catalyze protein synthesis, consist of a small 40S subunit and a large 60S subunit. Together these subunits are composed of 4 RNA species and approximately 80 structurally distinct proteins. This gene encodes a ribosomal protein that is a component of the 60S subunit. The protein belongs to the L30P family of ribosomal proteins. It contains an N-terminal basic region-leucine zipper (BZIP)-like domain and the RNP consensus submotif RNP2. In vitro the BZIP-like domain mediates homodimerization and stable binding to DNA and RNA, with a preference for 28S rRNA and mRNA. The protein can inhibit cell-free translation of mRNAs, suggesting that it plays a regulatory role in the translation apparatus. It is located in the cytoplasm. The protein has been shown to be an autoantigen in patients with systemic autoimmune diseases, such as systemic lupus erythematosus. As is typical for genes encoding ribosomal proteins, there are multiple processed pseudogenes of this gene dispersed through the genome.
, ribosomal protein L7
, 60S ribosomal protein L7