The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase

Samuel I. Gunderson; Katrin Beyer; Georges Martin; Water Keller; Wilbert C. Boelens; Iain W. Mattaj

doi:10.1016/0092-8674(94)90116-3

The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase

Samuel I. Gunderson, Katrin Beyer, Georges Martin, Water Keller, Wilbert C. Boelens, Iain W. Mattaj

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

181 Scopus citations

Abstract

The human U1 snRNP-specific U1A protein autoregulates its production by binding its own pre-mRNA and inhibiting polyadenylation. The mechanism of this regulation has been elucidated by in vitro studies. U1A protein is shown not to prevent either binding of cleavage and polyadenylation specificity factor (CPSF) to its recognition sequence (AUUAAA) or to prevent cleavage of U1A pre-mRNA. Instead, U1A protein bound to U1A pre-mRNA inhibits both specific and nonspecific polyadenylation by mammalian, but not by yeast, poly(A) polymerase (PAP). Domains are identified in both proteins whose removal uncouples the polyadenylation activity of mammalian PAP from its inhibition via RNA-bound U1A protein. Finally, U1A protein is shown to specifically interact with mammalian PAP in vitro. The possibility that this interaction may reflect a broader role of the U1A protein in polyadenylation is discussed.

Original language	English (US)
Pages (from-to)	531-541
Number of pages	11
Journal	Cell
Volume	76
Issue number	3
DOIs	https://doi.org/10.1016/0092-8674(94)90116-3
State	Published - Feb 11 1994
Externally published	Yes

All Science Journal Classification (ASJC) codes

Biochemistry, Genetics and Molecular Biology(all)

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10.1016/0092-8674(94)90116-3

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title = "The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase",

abstract = "The human U1 snRNP-specific U1A protein autoregulates its production by binding its own pre-mRNA and inhibiting polyadenylation. The mechanism of this regulation has been elucidated by in vitro studies. U1A protein is shown not to prevent either binding of cleavage and polyadenylation specificity factor (CPSF) to its recognition sequence (AUUAAA) or to prevent cleavage of U1A pre-mRNA. Instead, U1A protein bound to U1A pre-mRNA inhibits both specific and nonspecific polyadenylation by mammalian, but not by yeast, poly(A) polymerase (PAP). Domains are identified in both proteins whose removal uncouples the polyadenylation activity of mammalian PAP from its inhibition via RNA-bound U1A protein. Finally, U1A protein is shown to specifically interact with mammalian PAP in vitro. The possibility that this interaction may reflect a broader role of the U1A protein in polyadenylation is discussed.",

author = "Gunderson, {Samuel I.} and Katrin Beyer and Georges Martin and Water Keller and Boelens, {Wilbert C.} and Mattaj, {Iain W.}",

note = "Funding Information: The authors would like to thank P. Preker for yeast PAP; S. Bienroth for purified CPSF; E. Wahle for PAB II and calf thymus PAP; and M. Polycarpou-Schwarz for recombinant UlA protein. We would further like to thank members of our laboratories, especially E. Wahle, for valuable discussions, and C. Dargemont, C. Dingwall, M. Hentze, A. Lamond, J. Lewis, and B. Seraphin for comments on the manuscript. The work was supported in part by European Molecular Biology Laboratory, and in part by grants from the Canton of Base1 and the Swiss National Foundation. S. G. was the recipient of a von Humboldt postdoctoral fellowship.",

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AU - Gunderson, Samuel I.

AU - Beyer, Katrin

AU - Martin, Georges

AU - Keller, Water

AU - Boelens, Wilbert C.

AU - Mattaj, Iain W.

N1 - Funding Information: The authors would like to thank P. Preker for yeast PAP; S. Bienroth for purified CPSF; E. Wahle for PAB II and calf thymus PAP; and M. Polycarpou-Schwarz for recombinant UlA protein. We would further like to thank members of our laboratories, especially E. Wahle, for valuable discussions, and C. Dargemont, C. Dingwall, M. Hentze, A. Lamond, J. Lewis, and B. Seraphin for comments on the manuscript. The work was supported in part by European Molecular Biology Laboratory, and in part by grants from the Canton of Base1 and the Swiss National Foundation. S. G. was the recipient of a von Humboldt postdoctoral fellowship.

PY - 1994/2/11

Y1 - 1994/2/11

N2 - The human U1 snRNP-specific U1A protein autoregulates its production by binding its own pre-mRNA and inhibiting polyadenylation. The mechanism of this regulation has been elucidated by in vitro studies. U1A protein is shown not to prevent either binding of cleavage and polyadenylation specificity factor (CPSF) to its recognition sequence (AUUAAA) or to prevent cleavage of U1A pre-mRNA. Instead, U1A protein bound to U1A pre-mRNA inhibits both specific and nonspecific polyadenylation by mammalian, but not by yeast, poly(A) polymerase (PAP). Domains are identified in both proteins whose removal uncouples the polyadenylation activity of mammalian PAP from its inhibition via RNA-bound U1A protein. Finally, U1A protein is shown to specifically interact with mammalian PAP in vitro. The possibility that this interaction may reflect a broader role of the U1A protein in polyadenylation is discussed.

AB - The human U1 snRNP-specific U1A protein autoregulates its production by binding its own pre-mRNA and inhibiting polyadenylation. The mechanism of this regulation has been elucidated by in vitro studies. U1A protein is shown not to prevent either binding of cleavage and polyadenylation specificity factor (CPSF) to its recognition sequence (AUUAAA) or to prevent cleavage of U1A pre-mRNA. Instead, U1A protein bound to U1A pre-mRNA inhibits both specific and nonspecific polyadenylation by mammalian, but not by yeast, poly(A) polymerase (PAP). Domains are identified in both proteins whose removal uncouples the polyadenylation activity of mammalian PAP from its inhibition via RNA-bound U1A protein. Finally, U1A protein is shown to specifically interact with mammalian PAP in vitro. The possibility that this interaction may reflect a broader role of the U1A protein in polyadenylation is discussed.

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The human U1A snRNP protein regulates polyadenylation via a direct interaction with poly(A) polymerase

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