Entry - *602636 - PROTEIN PHOSPHATASE 1, REGULATORY SUBUNIT 8; PPP1R8 - OMIM
 
* 602636

PROTEIN PHOSPHATASE 1, REGULATORY SUBUNIT 8; PPP1R8


Alternative titles; symbols

NUCLEAR INHIBITOR OF PROTEIN PHOSPHATASE 1; NIPP1
ACTIVATOR OF RNA DECAY; ARD1
RNase E, E. COLI, HOMOLOG OF


HGNC Approved Gene Symbol: PPP1R8

Cytogenetic location: 1p35.3     Genomic coordinates (GRCh38): 1:27,830,782-27,851,676 (from NCBI)


TEXT

Cloning and Expression

In Escherichia coli, the rne gene encodes RNase E, a protein involved in RNA degradation. Wang and Cohen (1994) cloned a human gene, which they called ARD1 for 'activator of RNA decay,' that is able to complement mutations in the E. coli rne gene. The human ARD1 gene encodes a proline-rich 127-amino acid protein with a predicted mass of 13.3 kD. Wang and Cohen (1994) showed that human ARD1 protein is able to produce RNase E-specific cleavages in E. coli.

Van Eynde et al. (1995) cloned the bovine NIPP1 gene. The 351-amino acid NIPP1 protein is a specific inhibitor of type 1 serine/threonine protein phosphatases. The human ARD1 amino acid sequence is virtually identical to the carboxy terminus of the bovine NIPP1 amino acid sequence. Because the homology also extends into noncoding regions, the authors asserted that the NIPP1 and ARD1 proteins are alternately spliced products of the same gene.

Claverie-Martin et al. (1997) purified human ARD1 protein and found that its apparent size was 19 kD. They attributed the observed retarded mobility on SDS-PAGE to the highly charged residues at the ends of the protein. Enzyme assays showed that ARD1, like RNase E, is Mg2+ dependent and that ARD1 and RNase E cleave RNA at the same sites in A+U-rich regions.


Mapping

Wang (1995) showed that the common 3-prime untranslated region of ARD1 and NIPP1 maps to human chromosome 1.


REFERENCES

  1. Claverie-Martin, F., Wang, M., Cohen, S. N. ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E. J. Biol. Chem. 272: 13823-13828, 1997. [PubMed: 9153239, related citations] [Full Text]

  2. Van Eynde, A., Wera, S., Beullens, M., Torrekens, S., Van Leuven, F., Stalmans, W., Bollen, M. Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing. J. Biol. Chem. 270: 28068-28074, 1995. [PubMed: 7499293, related citations] [Full Text]

  3. Wang, M., Cohen, S. N. ard-1: a human gene that reverses the effects of temperature-sensitive and deletion mutations in the Escherichia coli rne gene and encodes an activity producing RNase E-like cleavages. Proc. Nat. Acad. Sci. 91: 10591-10595, 1994. [PubMed: 7524097, related citations] [Full Text]

  4. Wang, M. Isolation and characterization of a human gene encoding a single-strand-specific endoribonuclease. Ph.D. Thesis: Stanford Univ. 1995.


Creation Date:
Jennifer P. Macke : 5/18/1998
carol : 04/13/2021
alopez : 02/23/2000
carol : 4/14/1999
alopez : 10/28/1998
terry : 8/25/1998
alopez : 5/21/1998
alopez : 5/20/1998
alopez : 5/19/1998

* 602636

PROTEIN PHOSPHATASE 1, REGULATORY SUBUNIT 8; PPP1R8


Alternative titles; symbols

NUCLEAR INHIBITOR OF PROTEIN PHOSPHATASE 1; NIPP1
ACTIVATOR OF RNA DECAY; ARD1
RNase E, E. COLI, HOMOLOG OF


HGNC Approved Gene Symbol: PPP1R8

Cytogenetic location: 1p35.3     Genomic coordinates (GRCh38): 1:27,830,782-27,851,676 (from NCBI)


TEXT

Cloning and Expression

In Escherichia coli, the rne gene encodes RNase E, a protein involved in RNA degradation. Wang and Cohen (1994) cloned a human gene, which they called ARD1 for 'activator of RNA decay,' that is able to complement mutations in the E. coli rne gene. The human ARD1 gene encodes a proline-rich 127-amino acid protein with a predicted mass of 13.3 kD. Wang and Cohen (1994) showed that human ARD1 protein is able to produce RNase E-specific cleavages in E. coli.

Van Eynde et al. (1995) cloned the bovine NIPP1 gene. The 351-amino acid NIPP1 protein is a specific inhibitor of type 1 serine/threonine protein phosphatases. The human ARD1 amino acid sequence is virtually identical to the carboxy terminus of the bovine NIPP1 amino acid sequence. Because the homology also extends into noncoding regions, the authors asserted that the NIPP1 and ARD1 proteins are alternately spliced products of the same gene.

Claverie-Martin et al. (1997) purified human ARD1 protein and found that its apparent size was 19 kD. They attributed the observed retarded mobility on SDS-PAGE to the highly charged residues at the ends of the protein. Enzyme assays showed that ARD1, like RNase E, is Mg2+ dependent and that ARD1 and RNase E cleave RNA at the same sites in A+U-rich regions.


Mapping

Wang (1995) showed that the common 3-prime untranslated region of ARD1 and NIPP1 maps to human chromosome 1.


REFERENCES

  1. Claverie-Martin, F., Wang, M., Cohen, S. N. ARD-1 cDNA from human cells encodes a site-specific single-strand endoribonuclease that functionally resembles Escherichia coli RNase E. J. Biol. Chem. 272: 13823-13828, 1997. [PubMed: 9153239] [Full Text: https://doi.org/10.1074/jbc.272.21.13823]

  2. Van Eynde, A., Wera, S., Beullens, M., Torrekens, S., Van Leuven, F., Stalmans, W., Bollen, M. Molecular cloning of NIPP-1, a nuclear inhibitor of protein phosphatase-1, reveals homology with polypeptides involved in RNA processing. J. Biol. Chem. 270: 28068-28074, 1995. [PubMed: 7499293] [Full Text: https://doi.org/10.1074/jbc.270.47.28068]

  3. Wang, M., Cohen, S. N. ard-1: a human gene that reverses the effects of temperature-sensitive and deletion mutations in the Escherichia coli rne gene and encodes an activity producing RNase E-like cleavages. Proc. Nat. Acad. Sci. 91: 10591-10595, 1994. [PubMed: 7524097] [Full Text: https://doi.org/10.1073/pnas.91.22.10591]

  4. Wang, M. Isolation and characterization of a human gene encoding a single-strand-specific endoribonuclease. Ph.D. Thesis: Stanford Univ. 1995.


Creation Date:
Jennifer P. Macke : 5/18/1998

Edit History:
carol : 04/13/2021
alopez : 02/23/2000
carol : 4/14/1999
alopez : 10/28/1998
terry : 8/25/1998
alopez : 5/21/1998
alopez : 5/20/1998
alopez : 5/19/1998