Poly(A)-specific ribonuclease (PARN), also known as polyadenylate-specific ribonuclease or deadenylating nuclease (DAN), is an
enzyme that in humans is encoded by the PARNgene.[5][6]
Function
Exonucleolytic degradation of the
poly(A) tail is often the first step in the decay of eukaryotic
mRNAs. The amino acid sequence of poly(A)-specific ribonuclease shows homology to the
RNase D family of 3'-
exonucleases. The protein appears to be localized in both the nucleus and the cytoplasm. It is not stably associated with polysomes or ribosomal subunits.[6] Hereditary mutations in PARN lead to the bone marrow failure disease
dyskeratosis congenita which is caused by defective telomerase RNA processing and degradation in patients.[7][8][9][10][11][12][13]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Buiting K, Körner C, Ulrich B, Wahle E, Horsthemke B (May 2000). "The human gene for the poly(A)-specific ribonuclease (PARN) maps to 16p13 and has a truncated copy in the Prader-Willi/Angelman region on 15q11→q13". Cytogenetics and Cell Genetics. 87 (1–2): 125–31.
doi:
10.1159/000015378.
PMID10640832.
S2CID28498478.
^Dhanraj S, Gunja SM, Deveau AP, Nissbeck M, Boonyawat B, Coombs AJ, Renieri A, Mucciolo M, Marozza A, Buoni S, Turner L, Li H, Jarrar A, Sabanayagam M, Kirby M, Shago M, Pinto D, Berman JN, Scherer SW, Virtanen A, Dror Y (November 2015). "Bone marrow failure and developmental delay caused by mutations in poly(A)-specific ribonuclease (PARN)". Journal of Medical Genetics. 52 (11): 738–48.
doi:
10.1136/jmedgenet-2015-103292.
PMID26342108.
S2CID19822046.
Poly(A)-specific ribonuclease (PARN), also known as polyadenylate-specific ribonuclease or deadenylating nuclease (DAN), is an
enzyme that in humans is encoded by the PARNgene.[5][6]
Function
Exonucleolytic degradation of the
poly(A) tail is often the first step in the decay of eukaryotic
mRNAs. The amino acid sequence of poly(A)-specific ribonuclease shows homology to the
RNase D family of 3'-
exonucleases. The protein appears to be localized in both the nucleus and the cytoplasm. It is not stably associated with polysomes or ribosomal subunits.[6] Hereditary mutations in PARN lead to the bone marrow failure disease
dyskeratosis congenita which is caused by defective telomerase RNA processing and degradation in patients.[7][8][9][10][11][12][13]
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Buiting K, Körner C, Ulrich B, Wahle E, Horsthemke B (May 2000). "The human gene for the poly(A)-specific ribonuclease (PARN) maps to 16p13 and has a truncated copy in the Prader-Willi/Angelman region on 15q11→q13". Cytogenetics and Cell Genetics. 87 (1–2): 125–31.
doi:
10.1159/000015378.
PMID10640832.
S2CID28498478.
^Dhanraj S, Gunja SM, Deveau AP, Nissbeck M, Boonyawat B, Coombs AJ, Renieri A, Mucciolo M, Marozza A, Buoni S, Turner L, Li H, Jarrar A, Sabanayagam M, Kirby M, Shago M, Pinto D, Berman JN, Scherer SW, Virtanen A, Dror Y (November 2015). "Bone marrow failure and developmental delay caused by mutations in poly(A)-specific ribonuclease (PARN)". Journal of Medical Genetics. 52 (11): 738–48.
doi:
10.1136/jmedgenet-2015-103292.
PMID26342108.
S2CID19822046.