Identification of the heptameric Lsm complex that binds U6 snRNA in Trypanosoma brucei

Itai Dov Tkacz; Shlomo Cohen; Mali Salmon-Divon; Shulamit Michaeli

doi:10.1016/j.molbiopara.2008.03.003

Identification of the heptameric Lsm complex that binds U6 snRNA in Trypanosoma brucei

Itai Dov Tkacz
, Shlomo Cohen
, Mali Salmon-Divon
, Shulamit Michaeli

Bar-Ilan University

Research output: Contribution to journal › Article › peer-review

25 Scopus citations

Abstract

Lsm proteins are ubiquitous, multifunctional proteins that are involved in nuclear processing and turnover of many RNAs in eukaryotes. Lsm proteins form two distinct complexes, the Lsm2-8 complex, which binds U6 snRNA, and the Lsm1-7 complex, which governs mRNA degradation. Previously, seven Lsm proteins were identified in Trypanosoma brucei. Two of these proteins were later identified as SSm proteins (specific spliceosomal Sm proteins). In this study, the Lsm proteins (Lsm2 and Lsm5) that bind to U6 snRNA were identified. RNAi silencing and protein purification of TAP-tagged Lsm proteins were used to identify all the components of the trypanosome heptameric Lsm2-8 complex. Localization studies demonstrated that these proteins are found in the nucleus, near the nucleolus. Lsm proteins were not detected in cytoplasmic bodies that were tagged with YFP-Dhh1, which may suggest that in trypanosomes, Lsm-mediated degradation is not confined to such bodies.

Original language	English
Pages (from-to)	22-31
Number of pages	10
Journal	Molecular and Biochemical Parasitology
Volume	160
Issue number	1
DOIs	https://doi.org/10.1016/j.molbiopara.2008.03.003
State	Published - Jul 2008

Bibliographical note

Funding Information:
This study was supported by a United States–Israel Binational Science Foundation grant and by an International Research Scholar grant from the Howard Hughes Medical Institute to SM. SM holds the David and Inez Myers Chair in RNA silencing of diseases. We thank Dr. Mark Carrington (Cambridge University) for providing us the vector to perform the in situ YFP tagging and the YFP-Dhh1 cell line.

Funding

This study was supported by a United States–Israel Binational Science Foundation grant and by an International Research Scholar grant from the Howard Hughes Medical Institute to SM. SM holds the David and Inez Myers Chair in RNA silencing of diseases. We thank Dr. Mark Carrington (Cambridge University) for providing us the vector to perform the in situ YFP tagging and the YFP-Dhh1 cell line.

Funders
Howard Hughes Medical Institute
United States-Israel Binational Science Foundation

Keywords

Lsm
Trypanosoma brucei
U6 snRNA

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10.1016/j.molbiopara.2008.03.003

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title = "Identification of the heptameric Lsm complex that binds U6 snRNA in Trypanosoma brucei",

abstract = "Lsm proteins are ubiquitous, multifunctional proteins that are involved in nuclear processing and turnover of many RNAs in eukaryotes. Lsm proteins form two distinct complexes, the Lsm2-8 complex, which binds U6 snRNA, and the Lsm1-7 complex, which governs mRNA degradation. Previously, seven Lsm proteins were identified in Trypanosoma brucei. Two of these proteins were later identified as SSm proteins (specific spliceosomal Sm proteins). In this study, the Lsm proteins (Lsm2 and Lsm5) that bind to U6 snRNA were identified. RNAi silencing and protein purification of TAP-tagged Lsm proteins were used to identify all the components of the trypanosome heptameric Lsm2-8 complex. Localization studies demonstrated that these proteins are found in the nucleus, near the nucleolus. Lsm proteins were not detected in cytoplasmic bodies that were tagged with YFP-Dhh1, which may suggest that in trypanosomes, Lsm-mediated degradation is not confined to such bodies.",

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AU - Michaeli, Shulamit

N1 - Funding Information: This study was supported by a United States–Israel Binational Science Foundation grant and by an International Research Scholar grant from the Howard Hughes Medical Institute to SM. SM holds the David and Inez Myers Chair in RNA silencing of diseases. We thank Dr. Mark Carrington (Cambridge University) for providing us the vector to perform the in situ YFP tagging and the YFP-Dhh1 cell line.

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AB - Lsm proteins are ubiquitous, multifunctional proteins that are involved in nuclear processing and turnover of many RNAs in eukaryotes. Lsm proteins form two distinct complexes, the Lsm2-8 complex, which binds U6 snRNA, and the Lsm1-7 complex, which governs mRNA degradation. Previously, seven Lsm proteins were identified in Trypanosoma brucei. Two of these proteins were later identified as SSm proteins (specific spliceosomal Sm proteins). In this study, the Lsm proteins (Lsm2 and Lsm5) that bind to U6 snRNA were identified. RNAi silencing and protein purification of TAP-tagged Lsm proteins were used to identify all the components of the trypanosome heptameric Lsm2-8 complex. Localization studies demonstrated that these proteins are found in the nucleus, near the nucleolus. Lsm proteins were not detected in cytoplasmic bodies that were tagged with YFP-Dhh1, which may suggest that in trypanosomes, Lsm-mediated degradation is not confined to such bodies.

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Identification of the heptameric Lsm complex that binds U6 snRNA in Trypanosoma brucei

Abstract

Bibliographical note

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Keywords

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