scholarly journals RNA Metabolism Guided by RNA Modifications: The Role of SMUG1 in rRNA Quality Control

Biomolecules ◽  
2021 ◽  
Vol 11 (1) ◽  
pp. 76
Author(s):  
Lisa Lirussi ◽  
Özlem Demir ◽  
Panpan You ◽  
Antonio Sarno ◽  
Rommie E. Amaro ◽  
...  
Keyword(s):  
Quality Control ◽  
Excision Repair ◽  
Control Mechanisms ◽  
Rna Modifications ◽  
Pseudouridine Synthase ◽  
Repair Enzymes ◽  
Rna Quality Control ◽  
Eukaryotic Dna ◽  
Base Excision ◽  
Post Transcriptional Regulation

RNA modifications are essential for proper RNA processing, quality control, and maturation steps. In the last decade, some eukaryotic DNA repair enzymes have been shown to have an ability to recognize and process modified RNA substrates and thereby contribute to RNA surveillance. Single-strand-selective monofunctional uracil-DNA glycosylase 1 (SMUG1) is a base excision repair enzyme that not only recognizes and removes uracil and oxidized pyrimidines from DNA but is also able to process modified RNA substrates. SMUG1 interacts with the pseudouridine synthase dyskerin (DKC1), an enzyme essential for the correct assembly of small nucleolar ribonucleoproteins (snRNPs) and ribosomal RNA (rRNA) processing. Here, we review rRNA modifications and RNA quality control mechanisms in general and discuss the specific function of SMUG1 in rRNA metabolism. Cells lacking SMUG1 have elevated levels of immature rRNA molecules and accumulation of 5-hydroxymethyluridine (5hmU) in mature rRNA. SMUG1 may be required for post-transcriptional regulation and quality control of rRNAs, partly by regulating rRNA and stability.

scholarly journals The Human Base Excision Repair Enzyme SMUG1 Directly Interacts with DKC1 and Contributes to RNA Quality Control

2013 ◽  
Vol 49 (2) ◽  
pp. 339-345 ◽  
Author(s):  
Laure Jobert ◽  
Hanne K. Skjeldam ◽  
Bjørn Dalhus ◽  
Anastasia Galashevskaya ◽  
Cathrine Broberg Vågbø ◽  
...  
Keyword(s):  
Quality Control ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Repair Enzyme ◽  
Rna Quality ◽  
Rna Quality Control ◽  
Base Excision

scholarly journals The human checkpoint sensor and alternative DNA clamp Rad9–Rad1–Hus1 modulates the activity of DNA ligase I, a component of the long-patch base excision repair machinery

2005 ◽  
Vol 389 (1) ◽  
pp. 13-17 ◽  
Author(s):  
Ekaterina SMIRNOVA ◽  
Magali TOUEILLE ◽  
Enni MARKKANEN ◽  
Ulrich HÜBSCHER
Keyword(s):  
Quality Control ◽  
Dna Polymerase ◽  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Ligase ◽  
Dna Polymerase Β ◽  
Flap Endonuclease 1 ◽  
Important Target ◽  
Dna Ligase I ◽  
Base Excision

The human checkpoint sensor and alternative clamp Rad9–Rad1–Hus1 can interact with and specifically stimulate DNA ligase I. The very recently described interactions of Rad9–Rad1–Hus1 with MutY DNA glycosylase, DNA polymerase β and Flap endonuclease 1 now complete our view that the long-patch base excision machinery is an important target of the Rad9–Rad1–Hus1 complex, thus enhancing the quality control of DNA.

Oxidative base damage to DNA: specificity of base excision repair enzymes

2000 ◽  
Vol 462 (2-3) ◽  
pp. 121-128 ◽  
Author(s):  
Jean Cadet ◽  
Anne-Gaëlle Bourdat ◽  
Cédric D'Ham ◽  
Victor Duarte ◽  
Didier Gasparutto ◽  
...  
Keyword(s):  
Base Excision Repair ◽  
Excision Repair ◽  
Base Damage ◽  
Repair Enzymes ◽  
Base Excision ◽  
Dna Specificity ◽  
Oxidative Base Damage

Processing of the abasic sites clustered with the benzo[a]pyrene adducts by the base excision repair enzymes

DNA Repair ◽  
2017 ◽  
Vol 50 ◽  
pp. 43-53 ◽  
Author(s):  
Lidia V. Starostenko ◽  
Nadejda I. Rechkunova ◽  
Natalia A. Lebedeva ◽  
Alexander A. Lomzov ◽  
Vladimir V. Koval ◽  
...  
Keyword(s):  
Base Excision Repair ◽  
Excision Repair ◽  
Abasic Sites ◽  
Repair Enzymes ◽  
Base Excision

scholarly journals Formation of cytosine glycol and 5,6-dihydroxycytosine in deoxyribonucleic acid on treatment with osmium tetroxide

1986 ◽  
Vol 235 (2) ◽  
pp. 531-536 ◽  
Author(s):  
M Dizdaroglu ◽  
E Holwitt ◽  
M P Hagan ◽  
W F Blakely
Keyword(s):  
Dna Repair ◽  
Formic Acid ◽  
Excision Repair ◽  
Dna Lesions ◽  
Gas Chromatography Mass Spectrometry ◽  
Dna Glycosylases ◽  
Thymine Glycol ◽  
Repair Enzymes ◽  
Base Excision

OsO4 selectively forms thymine glycol lesions in DNA. In the past, OsO4-treated DNA has been used as a substrate in studies of DNA repair utilizing base-excision repair enzymes such as DNA glycosylases. There is, however, no information available on the chemical identity of other OsO4-induced base lesions in DNA. A complete knowledge of such DNA lesions may be of importance for repair studies. Using a methodology developed recently for characterization of oxidative base damage in DNA, we provide evidence for the formation of cytosine glycol and 5,6-dihydroxycytosine moieties, in addition to thymine glycol, in DNA on treatment with OsO4. For this purpose, samples of OsO4-treated DNA were hydrolysed with formic acid, then trimethylsilylated and analysed by capillary gas chromatography-mass spectrometry. In addition to thymine glycol, 5-hydroxyuracil (isobarbituric acid), 5-hydroxycytosine and 5,6-dihydroxyuracil (isodialuric acid or dialuric acid) were identified in OsO4-treated DNA. It is suggested that 5-hydroxyuracil was formed by formic acid-induced deamination and dehydration of cytosine glycol, which was the actual oxidation product of the cytosine moiety in DNA. 5-Hydroxycytosine obviously resulted from dehydration of cytosine glycol, and 5,6-dihydroxyuracil from deamination of 5,6-dihydroxycytosine. This scheme was supported by the presence of 5-hydroxyuracil, uracil glycol and 5,6-dihydroxyuracil in OsO4-treated cytosine. Treatment of OsO4-treated cytosine with formic acid caused the complete conversion of uracil glycol into 5-hydroxyuracil. The implications of these findings relative to studies of DNA repair are discussed.

Heat-Shock Proteins Associated with Base Excision Repair Enzymes in HeLa Cells

2000 ◽  
Vol 153 (2) ◽  
pp. 186-195 ◽  
Author(s):  
Frances Mendez ◽  
Margarita Sandigursky ◽  
William A. Franklin ◽  
Mark K. Kenny ◽  
Raichal Kureekattil ◽  
...  
Keyword(s):  
Heat Shock ◽  
Heat Shock Proteins ◽  
Base Excision Repair ◽  
Hela Cells ◽  
Excision Repair ◽  
Repair Enzymes ◽  
Base Excision ◽  
Shock Proteins

Response of Base Excision Repair Enzymes to Complex DNA Lesions

2001 ◽  
Vol 156 (5) ◽  
pp. 584-589 ◽  
Author(s):  
M. Weinfeld ◽  
A. Rasouli-Nia ◽  
M. A. Chaudhry ◽  
R. A. Britten
Keyword(s):  
Base Excision Repair ◽  
Excision Repair ◽  
Dna Lesions ◽  
Repair Enzymes ◽  
Base Excision

Roles of base excision repair enzymes Nth1p and Apn2p from Schizosaccharomyces pombe in processing alkylation and oxidative DNA damage

DNA Repair ◽  
2005 ◽  
Vol 4 (11) ◽  
pp. 1270-1280 ◽  
Author(s):  
Takanori Sugimoto ◽  
Emi Igawa ◽  
Haruna Tanihigashi ◽  
Mayumi Matsubara ◽  
Hiroshi Ide ◽  
...  
Keyword(s):  
Dna Damage ◽  
Schizosaccharomyces Pombe ◽  
Base Excision Repair ◽  
Oxidative Dna Damage ◽  
Excision Repair ◽  
Repair Enzymes ◽  
Base Excision
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