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Supramolecular complexes mediate selenocysteine incorporation in vivo.
Mol Cell Biol. 2006 Mar; 26(6):2337-46.MC

Abstract

Selenocysteine incorporation in eukaryotes occurs cotranslationally at UGA codons via the interactions of RNA-protein complexes, one comprised of selenocysteyl (Sec)-tRNA([Ser]Sec) and its specific elongation factor, EFsec, and another consisting of the SECIS element and SECIS binding protein, SBP2. Other factors implicated in this pathway include two selenophosphate synthetases, SPS1 and SPS2, ribosomal protein L30, and two factors identified as binding tRNA([Ser]Sec), termed soluble liver antigen/liver protein (SLA/LP) and SECp43. We report that SLA/LP and SPS1 interact in vitro and in vivo and that SECp43 cotransfection increases this interaction and redistributes all three proteins to a predominantly nuclear localization. We further show that SECp43 interacts with the selenocysteyl-tRNA([Ser]Sec)-EFsec complex in vitro, and SECp43 coexpression promotes interaction between EFsec and SBP2 in vivo. Additionally, SECp43 increases selenocysteine incorporation and selenoprotein mRNA levels, the latter presumably due to circumvention of nonsense-mediated decay. Thus, SECp43 emerges as a key player in orchestrating the interactions and localization of the other factors involved in selenoprotein biosynthesis. Finally, our studies delineating the multiple, coordinated protein-nucleic acid interactions between SECp43 and the previously described selenoprotein cotranslational factors resulted in a model of selenocysteine biosynthesis and incorporation dependent upon both cytoplasmic and nuclear supramolecular complexes.

Authors+Show Affiliations

Department of Cell and Molecular Biology, John A. Burns School of Medicine, University of Hawaii at Manoa, Honolulu, HI 96822, USA.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, N.I.H., Extramural

Language

eng

PubMed ID

16508009

Citation

Small-Howard, Andrea, et al. "Supramolecular Complexes Mediate Selenocysteine Incorporation in Vivo." Molecular and Cellular Biology, vol. 26, no. 6, 2006, pp. 2337-46.
Small-Howard A, Morozova N, Stoytcheva Z, et al. Supramolecular complexes mediate selenocysteine incorporation in vivo. Mol Cell Biol. 2006;26(6):2337-46.
Small-Howard, A., Morozova, N., Stoytcheva, Z., Forry, E. P., Mansell, J. B., Harney, J. W., Carlson, B. A., Xu, X. M., Hatfield, D. L., & Berry, M. J. (2006). Supramolecular complexes mediate selenocysteine incorporation in vivo. Molecular and Cellular Biology, 26(6), 2337-46.
Small-Howard A, et al. Supramolecular Complexes Mediate Selenocysteine Incorporation in Vivo. Mol Cell Biol. 2006;26(6):2337-46. PubMed PMID: 16508009.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - Supramolecular complexes mediate selenocysteine incorporation in vivo. AU - Small-Howard,Andrea, AU - Morozova,Nadya, AU - Stoytcheva,Zoia, AU - Forry,Erin P, AU - Mansell,John B, AU - Harney,John W, AU - Carlson,Bradley A, AU - Xu,Xue-Ming, AU - Hatfield,Dolph L, AU - Berry,Marla J, PY - 2006/3/2/pubmed PY - 2006/6/21/medline PY - 2006/3/2/entrez SP - 2337 EP - 46 JF - Molecular and cellular biology JO - Mol. Cell. Biol. VL - 26 IS - 6 N2 - Selenocysteine incorporation in eukaryotes occurs cotranslationally at UGA codons via the interactions of RNA-protein complexes, one comprised of selenocysteyl (Sec)-tRNA([Ser]Sec) and its specific elongation factor, EFsec, and another consisting of the SECIS element and SECIS binding protein, SBP2. Other factors implicated in this pathway include two selenophosphate synthetases, SPS1 and SPS2, ribosomal protein L30, and two factors identified as binding tRNA([Ser]Sec), termed soluble liver antigen/liver protein (SLA/LP) and SECp43. We report that SLA/LP and SPS1 interact in vitro and in vivo and that SECp43 cotransfection increases this interaction and redistributes all three proteins to a predominantly nuclear localization. We further show that SECp43 interacts with the selenocysteyl-tRNA([Ser]Sec)-EFsec complex in vitro, and SECp43 coexpression promotes interaction between EFsec and SBP2 in vivo. Additionally, SECp43 increases selenocysteine incorporation and selenoprotein mRNA levels, the latter presumably due to circumvention of nonsense-mediated decay. Thus, SECp43 emerges as a key player in orchestrating the interactions and localization of the other factors involved in selenoprotein biosynthesis. Finally, our studies delineating the multiple, coordinated protein-nucleic acid interactions between SECp43 and the previously described selenoprotein cotranslational factors resulted in a model of selenocysteine biosynthesis and incorporation dependent upon both cytoplasmic and nuclear supramolecular complexes. SN - 0270-7306 UR - https://www.unboundmedicine.com/medline/citation/16508009/Supramolecular_complexes_mediate_selenocysteine_incorporation_in_vivo_ L2 - http://mcb.asm.org/cgi/pmidlookup?view=long&pmid=16508009 DB - PRIME DP - Unbound Medicine ER -