The complete primary structure of the human snRNP E protein

David R. Stanford; Maria Kehl; Caroline A. Perry; Eileen L. Holicky; Scott E. Harvey; Anne M. Rohleder; Kai Render; Reinhard Luhrmann; Eric D. Wieben

doi:10.1093/nar/16.22.10593

The complete primary structure of the human snRNP E protein

David R. Stanford, Maria Kehl, Caroline A. Perry, Eileen L. Holicky, Scott E. Harvey, Anne M. Rohleder, Kai Render, Reinhard Luhrmann, Eric D. Wieben

Biochemistry and Molecular Biology

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

28 Scopus citations

Abstract

The snRNP E protein is one of four "core" proteins associated with the snRNAs of the U family (U1,U2,U4,U5, and U6). Screening of a human teratoma cDNA library with a partial cDNA for a human autoimmune antigen resulted in the isolation of a cDNA clone containing the entire coding region of this snRNP core protein. Comparison of the 5′ end of this cDNA with the sequences of two processed pseudogenes and primer extension data suggest that the cDNA is nearly full length. The longest open reading frame in this clone codes for a basic 92 amino acid protein which is in perfect agreement with amino acid sequence data obtained from purified E protein. The predicted sequence of this protein reveals no extensive similarity to other snRNP proteins, but contains regions of similarity to a eukaryotic ribosomal protein.

Original language	English (US)
Pages (from-to)	10593-10605
Number of pages	13
Journal	Nucleic acids research
Volume	16
Issue number	22
DOIs	https://doi.org/10.1093/nar/16.22.10593
State	Published - Nov 25 1988

ASJC Scopus subject areas

Genetics

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title = "The complete primary structure of the human snRNP E protein",

abstract = "The snRNP E protein is one of four {"}core{"} proteins associated with the snRNAs of the U family (U1,U2,U4,U5, and U6). Screening of a human teratoma cDNA library with a partial cDNA for a human autoimmune antigen resulted in the isolation of a cDNA clone containing the entire coding region of this snRNP core protein. Comparison of the 5′ end of this cDNA with the sequences of two processed pseudogenes and primer extension data suggest that the cDNA is nearly full length. The longest open reading frame in this clone codes for a basic 92 amino acid protein which is in perfect agreement with amino acid sequence data obtained from purified E protein. The predicted sequence of this protein reveals no extensive similarity to other snRNP proteins, but contains regions of similarity to a eukaryotic ribosomal protein.",

author = "Stanford, {David R.} and Maria Kehl and Perry, {Caroline A.} and Holicky, {Eileen L.} and Harvey, {Scott E.} and Rohleder, {Anne M.} and Kai Render and Reinhard Luhrmann and Wieben, {Eric D.}",

note = "Funding Information: ACKNOWLEDGEMENTS We appreciate the generous gifts of the human genomic library from Dr. T. Maniatis and the human teratoma cDNA library from Dr. J. Skowronski. We would also like to thank J. Greene for assistance with primer extensions. This work was supported by NTH Grants AR38554 and CA09441 to E.D.W. and D.R.S., a grant from the Deutsche Forschungsgemeinschaft to R.L. (Lu 294/2-2) and in part by the Mayo Foundation (E.D.W.).",

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AU - Perry, Caroline A.

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AU - Harvey, Scott E.

AU - Rohleder, Anne M.

AU - Render, Kai

AU - Luhrmann, Reinhard

AU - Wieben, Eric D.

N1 - Funding Information: ACKNOWLEDGEMENTS We appreciate the generous gifts of the human genomic library from Dr. T. Maniatis and the human teratoma cDNA library from Dr. J. Skowronski. We would also like to thank J. Greene for assistance with primer extensions. This work was supported by NTH Grants AR38554 and CA09441 to E.D.W. and D.R.S., a grant from the Deutsche Forschungsgemeinschaft to R.L. (Lu 294/2-2) and in part by the Mayo Foundation (E.D.W.).

PY - 1988/11/25

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N2 - The snRNP E protein is one of four "core" proteins associated with the snRNAs of the U family (U1,U2,U4,U5, and U6). Screening of a human teratoma cDNA library with a partial cDNA for a human autoimmune antigen resulted in the isolation of a cDNA clone containing the entire coding region of this snRNP core protein. Comparison of the 5′ end of this cDNA with the sequences of two processed pseudogenes and primer extension data suggest that the cDNA is nearly full length. The longest open reading frame in this clone codes for a basic 92 amino acid protein which is in perfect agreement with amino acid sequence data obtained from purified E protein. The predicted sequence of this protein reveals no extensive similarity to other snRNP proteins, but contains regions of similarity to a eukaryotic ribosomal protein.

AB - The snRNP E protein is one of four "core" proteins associated with the snRNAs of the U family (U1,U2,U4,U5, and U6). Screening of a human teratoma cDNA library with a partial cDNA for a human autoimmune antigen resulted in the isolation of a cDNA clone containing the entire coding region of this snRNP core protein. Comparison of the 5′ end of this cDNA with the sequences of two processed pseudogenes and primer extension data suggest that the cDNA is nearly full length. The longest open reading frame in this clone codes for a basic 92 amino acid protein which is in perfect agreement with amino acid sequence data obtained from purified E protein. The predicted sequence of this protein reveals no extensive similarity to other snRNP proteins, but contains regions of similarity to a eukaryotic ribosomal protein.

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The complete primary structure of the human snRNP E protein

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