Entry - *600369 - CLEAVAGE STIMULATION FACTOR, 3-PRIME PRE-RNA, SUBUNIT 1, 50-KD; CSTF1 - OMIM
 
* 600369

CLEAVAGE STIMULATION FACTOR, 3-PRIME PRE-RNA, SUBUNIT 1, 50-KD; CSTF1


HGNC Approved Gene Symbol: CSTF1

Cytogenetic location: 20q13.2-q13.31     Genomic coordinates (GRCh38): 20:56,392,379-56,406,362 (from NCBI)


TEXT

Cloning and Expression

Polyadenylation of mRNA is a complex process that requires multiple protein factors, including 3 cleavage stimulation factors (CSTF1; CSFT2, 300907; and CSTF3, 600367). CstF1, a 50-kD protein cloned by Takagaki and Manley (1992), contains transducin-like repeats characteristic of mammalian G protein beta subunits.


Gene Function

Kleiman and Manley (1999) demonstrated that CSTF1 interacts in vitro and in intact cells with BARD1 (601593). The BARD1-CSTF1 interaction inhibited polyadenylation in vitro. BARD1, like CSTF1, interacts with RNA polymerase-2. BARD1, BRCA1, and CSTF1 were shown to associate in vivo. Kleiman and Manley (1999) demonstrated that BARD1 inhibits pre-mRNA 3-prime cleavage in vitro and that the same region of BARD1 required for binding of CSTF1 is necessary for inhibiting 3-prime pre-mRNA cleavage. Kleiman and Manley (1999) concluded that their results suggested a model in which BARD1, as part of the RNA polymerase-2 holoenzyme, senses sites of DNA damage and repair, and the inhibitory interaction with CSTF1 ensures that nascent RNAs are not erroneously polyadenylated at such sites.


REFERENCES

  1. Kleiman, F. E., Manley, J. L. Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50. Science 285: 1576-1579, 1999. [PubMed: 10477523, related citations] [Full Text]

  2. Takagaki, Y., Manley, J. L. A human polyadenylation factor is a G protein beta-subunit homologue. J. Biol. Chem. 267: 23471-23474, 1992. [PubMed: 1358884, related citations]


Contributors:
Ada Hamosh - updated : 9/2/1999
Creation Date:
Victor A. McKusick : 2/3/1995
alopez : 04/08/2014
mgross : 10/16/2013
alopez : 9/2/1999
alopez : 9/2/1999
alopez : 12/15/1998
terry : 6/3/1998
carol : 2/3/1995

* 600369

CLEAVAGE STIMULATION FACTOR, 3-PRIME PRE-RNA, SUBUNIT 1, 50-KD; CSTF1


HGNC Approved Gene Symbol: CSTF1

Cytogenetic location: 20q13.2-q13.31     Genomic coordinates (GRCh38): 20:56,392,379-56,406,362 (from NCBI)


TEXT

Cloning and Expression

Polyadenylation of mRNA is a complex process that requires multiple protein factors, including 3 cleavage stimulation factors (CSTF1; CSFT2, 300907; and CSTF3, 600367). CstF1, a 50-kD protein cloned by Takagaki and Manley (1992), contains transducin-like repeats characteristic of mammalian G protein beta subunits.


Gene Function

Kleiman and Manley (1999) demonstrated that CSTF1 interacts in vitro and in intact cells with BARD1 (601593). The BARD1-CSTF1 interaction inhibited polyadenylation in vitro. BARD1, like CSTF1, interacts with RNA polymerase-2. BARD1, BRCA1, and CSTF1 were shown to associate in vivo. Kleiman and Manley (1999) demonstrated that BARD1 inhibits pre-mRNA 3-prime cleavage in vitro and that the same region of BARD1 required for binding of CSTF1 is necessary for inhibiting 3-prime pre-mRNA cleavage. Kleiman and Manley (1999) concluded that their results suggested a model in which BARD1, as part of the RNA polymerase-2 holoenzyme, senses sites of DNA damage and repair, and the inhibitory interaction with CSTF1 ensures that nascent RNAs are not erroneously polyadenylated at such sites.


REFERENCES

  1. Kleiman, F. E., Manley, J. L. Functional interaction of BRCA1-associated BARD1 with polyadenylation factor CstF-50. Science 285: 1576-1579, 1999. [PubMed: 10477523] [Full Text: https://doi.org/10.1126/science.285.5433.1576]

  2. Takagaki, Y., Manley, J. L. A human polyadenylation factor is a G protein beta-subunit homologue. J. Biol. Chem. 267: 23471-23474, 1992. [PubMed: 1358884]


Contributors:
Ada Hamosh - updated : 9/2/1999

Creation Date:
Victor A. McKusick : 2/3/1995

Edit History:
alopez : 04/08/2014
mgross : 10/16/2013
alopez : 9/2/1999
alopez : 9/2/1999
alopez : 12/15/1998
terry : 6/3/1998
carol : 2/3/1995