SMUG1
SMUG1 (single-strand-selective monofunctional uracil-DNA glycosylase 1, also known as UNG3, FDG and HMUDG) is a nuclear DNA glycosylase that recognises base lesions and initiates base excision repair. It removes uracil and oxidised uracil derivatives from DNA. Browse Assay Genie's current range of SMUG1 research reagents below, or read on for the biology behind the target.
SMUG1 recognises base lesions in the genome and initiates base excision DNA repair. It acts as a monofunctional DNA glycosylase specific for uracil (U) residues in DNA, with a preference for single-stranded substrates. Its activity is greater toward U/G mismatches than U/A matches. Besides uracil, the enzyme excises 5-formyluracil, 5-hydroxyuracil and 5-hydroxymethyluracil from both single-stranded and double-stranded DNA. It does not act on the analogous cytosine derivatives, 5-hydroxycytosine and 5-formylcytosine, or on other oxidised bases.
The activity of SMUG1 is damage-specific and salt-dependent. At low salt concentration the substrate preference is single-stranded DNA over double-stranded DNA with a G or A pair. At high salt concentration the order changes to double-stranded DNA with a G pair, then with an A pair, then single-stranded DNA. This makes buffer conditions an important consideration when designing activity assays for the enzyme.
The SMUG1 gene encodes a protein that belongs to the uracil-DNA glycosylase (UDG) superfamily and the SMUG1 family, and HGNC classifies it within the DNA glycosylases gene group. NCBI Gene notes that many alternatively spliced transcript variants exist, although the full-length nature is known for only some of them. The protein is localised to the nucleus. Mouse and rat orthologues are both named Smug1, which allows comparative work in rodent models.
SMUG1 removes uracil from single- and double-stranded DNA and initiates base excision repair, making it a central enzyme for studying this pathway.
The enzyme excises 5-formyluracil, 5-hydroxyuracil and 5-hydroxymethyluracil, so it is relevant to research on oxidative damage to uracil derivatives in DNA.
Its preference for single-stranded DNA and for U/G mismatches, plus its salt-dependent behaviour, makes SMUG1 a useful model of substrate selection among glycosylases.
As a member of the UDG superfamily and SMUG1 family, it supports comparative studies of how related glycosylases recognise and remove uracil.
SMUG1 is a monofunctional DNA glycosylase that recognises uracil and certain oxidised uracil derivatives in DNA and removes them, initiating base excision repair. It prefers single-stranded substrates and shows greater activity toward U/G mismatches than U/A matches.
The HGNC name is single-strand-selective monofunctional uracil-DNA glycosylase 1. Aliases and previous symbols include UNG3, FDG and HMUDG. NCBI Gene also reports many alternatively spliced transcript variants, though the full-length nature is known for only some of them.
Yes. Mouse and rat both have a Smug1 orthologue. The protein belongs to the SMUG1 family within the uracil-DNA glycosylase superfamily. Check the datasheet of any product for its validated reactivity.
Other DNA glycosylases and base excision repair proteins with products at Assay Genie.
Gene and protein annotations from HGNC, NCBI Gene and UniProt Q53HV7; product specifications from Assay Genie datasheets.