High impact information on RPS15

• By tracking the nuclear exit of this precursor, we have identified the ribosomal protein Rps15 as a determinant of preribosomal nuclear export in human cells [1].
• Most pre-40S specific factors are correctly associated with the intermediate particles accumulating in the nucleus upon Rps15p depletion, except the late-binding proteins Tsr1p and Rio2p [2].
• Enforced expression of ShIF in MS10 cells, bone marrow stroma cells that do not express endogenous ShIF or ISF, conferred on the cells an ability to support the growth of S21 cells as well as bone marrow cells [3].
• Protein YS25 and its counterparts, SP-S28 and rat S21 [nomenclature according to Sherton, C. C., & Wool, I. G. (1972) J. Biol. Chem. 247, 4460-4467], from Saccharomyces cerevisiae, Schizosaccharomyces pombe, and rat liver cytoplasmic ribosomes, respectively, were sequenced by a combination of various enzymatic digestions and/or chemical cleavage [4].
• The Arabidopsis S15 protein described here is about 75% identical to vertebrate S15, 70% identical to the homologous yeast protein (S21), 50% identical to archaebacterial S19, 30% identical to eubacterial S19, and about 30% identical to plant mitochondrial and plastid S19 [5].

Associations of RPS15 with chemical compounds

• Proteins S7, S10, S13, S21, S22 and S27 in the small subunit and L2/3, L5, L10/12, L19/20, L22, L23, L36/37, L42 and L43' in the large subunit are labelled when cross linked to [14C]spermidine using 1,5-difluoro 2,4-dinitrobenzene and are good candidates to be RNA-binding proteins in ribosomes from Saccharomyces cerevisiae [6].

Analytical, diagnostic and therapeutic context of RPS15

• On two-dimensional gel electrophoresis, the in vitro transcription/translation product of yeast rig cDNA co-migrated with yeast ribosomal protein S21 [7].

References