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Gene Review

Secisbp2  -  SECIS binding protein 2

Mus musculus

Synonyms: 2210413N07Rik, 2810012K13Rik, SBP2
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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].


  1. The transfer of a bacterial transmembrane function to eukaryotic cells. Lo, T.C. J. Biol. Chem. (1979) [Pubmed]
  2. Studies on the antineoplasticity of Schiff bases containing 5-nitrofuran and pyrimidine. Sur, B., Chatterjee, S.P., Sur, P., Maity, T., Roychoudhury, S. Oncology (1990) [Pubmed]
  3. Nuclear assembly of UGA decoding complexes on selenoprotein mRNAs: a mechanism for eluding nonsense-mediated decay? de Jesus, L.A., Hoffmann, P.R., Michaud, T., Forry, E.P., Small-Howard, A., Stillwell, R.J., Morozova, N., Harney, J.W., Berry, M.J. Mol. Cell. Biol. (2006) [Pubmed]
  4. The selenocysteine incorporation machinery: interactions between the SECIS RNA and the SECIS-binding protein SBP2. Fletcher, J.E., Copeland, P.R., Driscoll, D.M., Krol, A. RNA (2001) [Pubmed]
  5. A unique Babesia bovis spherical body protein is conserved among geographic isolates and localizes to the infected erythrocyte membrane. Ruef, B.J., Dowling, S.C., Conley, P.G., Perryman, L.E., Brown, W.C., Jasmer, D.P., Rice-Ficht, A.C. Mol. Biochem. Parasitol. (2000) [Pubmed]
  6. The rat growth hormone proximal silencer contains a novel DNA-binding site for multiple nuclear proteins that represses basal promoter activity. Roy, R.J., Vallières, L., Leclerc, S., Guérin, S.L. Eur. J. Biochem. (1994) [Pubmed]
  7. Polysome distribution of phospholipid hydroperoxide glutathione peroxidase mRNA: evidence for a block in elongation at the UGA/selenocysteine codon. Fletcher, J.E., Copeland, P.R., Driscoll, D.M. RNA (2000) [Pubmed]
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