Disease relevance of Secisbp2

• Purified dicarboxylate membrane transport components (SBP 1 and SBP 2) from Escherichia coli K12 were added to rat myoblasts and mouse L-cells [1].
• Doubling time, rates of protein and DNA synthesis inhibition and LD50 values-1,000 mg/kg body weight for SBP1 and 1,275 mg/kg body weight for 2-(5-nitro-2-furfurylidene-amino)-4- methylpyrimidine (SBP2)- in the oral route support the activity and use of SBP1 and SBP2 as future anticancer agents [2].

High impact information on Secisbp2

• In eukaryotes, two factors that are crucial to this recoding process are the mRNA binding protein of the Sec insertion sequence, SBP2, and the specialized elongation factor, EFsec [3].
• Intriguingly, both EFsec and SBP2 localization differed depending on the cell line but significant colocalization of the two proteins was observed in cells where SBP2 levels were detectable [3].
• We propose a model in which SBP2 covers the central part of the SECIS RNA, binding to the non-Watson-Crick base pair quartet and to the 5' strands of the lower helix and internal loop [4].
• In this study, we define the binding site of SBP2 on six different SECIS RNAs using enzymatic and hydroxyl radical footprinting, gel mobility shift analysis, and phosphate-ethylation binding interference [4].
• Modification of phosphates by ethylnitrosourea along both strands of the non-Watson-Crick base pair quartet, on the 5' strand of the lower helix and part of the 5' strand of the internal loop, prevented binding of SBP2 [4].

Biological context of Secisbp2

• Analysis of the SBP3 amino acid sequence revealed no significant amino acid identity to SBP1 and SBP2 and a lack of repeated epitopes, a notable feature of the other two spherical body proteins [5].
• A common recognition site for three yet uncharacterized nuclear proteins (designated as SBP1, SBP2 and SBP3) which bind a DNA sequence adjacent to the NF1-L-binding site in the rGH silencer-1 element were identified [6].

Anatomical context of Secisbp2

• Addition of SECIS-binding protein SBP2, which is essential for Sec insertion, increased ribosome loading and translation of wild-type PHGPx mRNA, but had no effect on the mutant mRNAs [7].

Analytical, diagnostic and therapeutic context of Secisbp2

• Gel mobility shift assays showed that the G.A/A.G tandem and internal loop are critical for the binding of SBP2 [4].
• Immunofluorescence studies showed binding of the 70/52.9 mAb to the infected-erythrocyte membrane region but not to their uninfected counterparts, demonstrating a host-cell association shared with the previously isolated B. bovis spherical body proteins, SBP1 and SBP2 [5].

References