LIF1/YGL090W Summary Help

Standard Name LIF1 1
Systematic Name YGL090W
Feature Type ORF, Verified
Description Component of the DNA ligase IV complex; this complex mediates nonhomologous end joining in DNA double-strand break repair; physically interacts with Dnl4p and Nej1p; homologous to mammalian XRCC4 protein (1, 2, 3 and see Summary Paragraph)
Name Description Ligase Interacting Factor 1
Chromosomal Location
ChrVII:343319 to 344584 | ORF Map | GBrowse
Gene Ontology Annotations All LIF1 GO evidence and references
  View Computational GO annotations for LIF1
Molecular Function
Manually curated
Biological Process
Manually curated
Cellular Component
Manually curated
Regulators 2 genes
Classical genetics
Large-scale survey
61 total interaction(s) for 28 unique genes/features.
Physical Interactions
  • Affinity Capture-MS: 8
  • Affinity Capture-RNA: 1
  • Affinity Capture-Western: 9
  • Co-crystal Structure: 1
  • Co-fractionation: 1
  • Co-purification: 2
  • Reconstituted Complex: 1
  • Two-hybrid: 23

Genetic Interactions
  • Negative Genetic: 5
  • Phenotypic Enhancement: 1
  • Phenotypic Suppression: 1
  • Positive Genetic: 2
  • Synthetic Growth Defect: 4
  • Synthetic Rescue: 2

Expression Summary
Length (a.a.) 421
Molecular Weight (Da) 48,259
Isoelectric Point (pI) 4.69
Phosphorylation PhosphoGRID | PhosphoPep Database
sequence information
ChrVII:343319 to 344584 | ORF Map | GBrowse
Last Update Coordinates: 2011-02-03 | Sequence: 1996-07-31
Subfeature details
Most Recent Updates
Coordinates Sequence
CDS 1..1266 343319..344584 2011-02-03 1996-07-31
Retrieve sequences
Analyze Sequence
S288C only
S288C vs. other species
S288C vs. other strains
External Links All Associated Seq | Entrez Gene | Entrez RefSeq Protein | MIPS | Search all NCBI (Entrez) | UniProtKB
Primary SGDIDS000003058

Lif1p is required for targeting Dnl4p to double-strand break sites non-homologous end-joining (NHEJ) (1, 2). Lif1p assembles as part of the NHEJ machinery at sites of double-strand breaks (DSBs) (4, 5, 6). This machinery is required to align and process the DSBs in preparation for ligation by Dnl4p (reviewed in 7, 8). Lif1p interacts with the BRCT domain of Dnl4p (1, 9). This interaction is required for the stability and DNA ligase activity of Dnl4p (1, 2). The nuclear localization of Lif1p may be regulated by Nej1p (10). lif1 mutants undergo meiosis and sporulation less efficiently than wild type cells (1).

Lif1p is widely conserved and is known as XRCC4 in humans (1, 9). Lif1p has sequence similarity with human XRCC4 in the region that interacts with the BRCT domain of Dnl4p (1).

Last updated: 2007-07-12 Contact SGD

References cited on this page View Complete Literature Guide for LIF1
1) Herrmann G, et al.  (1998) Saccharomyces cerevisiae LIF1: a function involved in DNA double-strand break repair related to mammalian XRCC4. EMBO J 17(14):4188-98
2) Teo SH and Jackson SP  (2000) Lif1p targets the DNA ligase Lig4p to sites of DNA double-strand breaks. Curr Biol 10(3):165-8
3) Deshpande RA and Wilson TE  (2007) Modes of interaction among yeast Nej1, Lif1 and Dnl4 proteins and comparison to human XLF, XRCC4 and Lig4. DNA Repair (Amst) 6(10):1507-16
4) Chen L, et al.  (2001) Promotion of Dnl4-catalyzed DNA end-joining by the Rad50/Mre11/Xrs2 and Hdf1/Hdf2 complexes. Mol Cell 8(5):1105-15
5) Tseng HM and Tomkinson AE  (2004) Processing and joining of DNA ends coordinated by interactions among Dnl4/Lif1, Pol4, and FEN-1. J Biol Chem 279(46):47580-8
6) Zhang Y, et al.  (2007) Role of Dnl4-Lif1 in nonhomologous end-joining repair complex assembly and suppression of homologous recombination. Nat Struct Mol Biol 14(7):639-46
7) Daley JM, et al.  (2005) Nonhomologous end joining in yeast. Annu Rev Genet 39():431-51
8) Hefferin ML and Tomkinson AE  (2005) Mechanism of DNA double-strand break repair by non-homologous end joining. DNA Repair (Amst) 4(6):639-48
9) Dore AS, et al.  (2006) Structure of an Xrcc4-DNA ligase IV yeast ortholog complex reveals a novel BRCT interaction mode. DNA Repair (Amst) 5(3):362-8
10) Valencia M, et al.  (2001) NEJ1 controls non-homologous end joining in Saccharomyces cerevisiae. Nature 414(6864):666-9