BMRP is a Bcl-2 binding protein that induces apoptosis

Sudhakar R. Chintharlapalli, Madhuri Jasti, Srinivas Malladi, Kishore V.L. Parsa, Rafael P. Ballestero, Maribel González-García

Research output: Contribution to journalArticle

29 Citations (Scopus)

Abstract

Members of the Bcl-2 family of proteins play important roles in the regulation of cell death by apoptosis. The yeast Two-Hybrid system was utilized to identify a protein that interacts with the anti-apoptotic protein Bcl-2, designated BMRP. This protein corresponds to a previously known mitochondrial ribosomal protein (MRPL41). Binding experiments confirmed the interaction of BMRP to Bcl-2 in mammalian cells. Subcellular fractionation by differential centrifugation studies showed that both Bcl-2 and BMRP are localized to the same fractions (fractions that are rich in mitochondria). Northern blot analysis revealed a major bmrp mRNA band of approximately 0.8 kb in several human tissues. Additionally, a larger 2.2 kb mRNA species was also observed in some tissues. Western blot analysis showed that endogenous BMRP runs as a band of 16-17 kDa in SDS-PAGE. Overexpression of BMRP induced cell death in primary embryonic fibroblasts and NIH/3T3 cells. Transfection of BMRP showed similar effects to those observed by overexpression of the pro-apoptotic proteins Bax or Bad. BMRP-stimulated cell death was counteracted by co-expression of Bcl-2. The baculoviral caspase inhibitor p35 also protected cells from BMRP-induced cell death. These findings suggest that BMRP is a mitochondrial ribosomal protein involved in the regulation of cell death by apoptosis, probably affecting pathways mediated by Bcl-2 and caspases.

Original languageEnglish (US)
Pages (from-to)611-626
Number of pages16
JournalJournal of Cellular Biochemistry
Volume94
Issue number3
DOIs
StatePublished - Feb 15 2005

Fingerprint

Cell death
Carrier Proteins
Cell Death
Apoptosis
Apoptosis Regulatory Proteins
Ribosomal Proteins
Mitochondrial Proteins
Caspase 2
Tissue
NIH 3T3 Cells
Messenger RNA
Two-Hybrid System Techniques
Proteins
Mitochondria
Caspase Inhibitors
Centrifugation
Fibroblasts
Fractionation
Hybrid systems
Northern Blotting

Keywords

  • Apoptosis
  • Bcl-2
  • BMRP
  • Mitochondria
  • Ribosome
  • Yeast Two-Hybrid screen

ASJC Scopus subject areas

  • Biochemistry
  • Molecular Biology
  • Cell Biology

Cite this

Chintharlapalli, S. R., Jasti, M., Malladi, S., Parsa, K. V. L., Ballestero, R. P., & González-García, M. (2005). BMRP is a Bcl-2 binding protein that induces apoptosis. Journal of Cellular Biochemistry, 94(3), 611-626. https://doi.org/10.1002/jcb.20292

BMRP is a Bcl-2 binding protein that induces apoptosis. / Chintharlapalli, Sudhakar R.; Jasti, Madhuri; Malladi, Srinivas; Parsa, Kishore V.L.; Ballestero, Rafael P.; González-García, Maribel.

In: Journal of Cellular Biochemistry, Vol. 94, No. 3, 15.02.2005, p. 611-626.

Research output: Contribution to journalArticle

Chintharlapalli, SR, Jasti, M, Malladi, S, Parsa, KVL, Ballestero, RP & González-García, M 2005, 'BMRP is a Bcl-2 binding protein that induces apoptosis', Journal of Cellular Biochemistry, vol. 94, no. 3, pp. 611-626. https://doi.org/10.1002/jcb.20292
Chintharlapalli SR, Jasti M, Malladi S, Parsa KVL, Ballestero RP, González-García M. BMRP is a Bcl-2 binding protein that induces apoptosis. Journal of Cellular Biochemistry. 2005 Feb 15;94(3):611-626. https://doi.org/10.1002/jcb.20292
Chintharlapalli, Sudhakar R. ; Jasti, Madhuri ; Malladi, Srinivas ; Parsa, Kishore V.L. ; Ballestero, Rafael P. ; González-García, Maribel. / BMRP is a Bcl-2 binding protein that induces apoptosis. In: Journal of Cellular Biochemistry. 2005 ; Vol. 94, No. 3. pp. 611-626.
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