COMMENTARY Open Access
Fanconi-like crosslink repair in yeast
Danielle L Daee and Kyungjae Myung*
Interstrand crosslinks covalently link complementary DNA strands, block replication and transcription, and can trigger
cell death. In eukaryotic systems several pathways, including the Fanconi Anemia pathway, are involved in repairing
interstrand crosslinks, but their precise mechanisms remain enigmatic. The lack of functional homologs in simpler
model organisms has significantly hampered progress in this field. Two recent studies have finally identified a
Fanconi-like interstrand crosslink repair pathway in yeast. Future studies in this simplistic model organism promise to
greatly improve our basic understanding of complex interstrand crosslink repair pathways like the Fanconi pathway.
Keywords: Fanconi anemia, Interstrand crosslink repair, Mph1, Chl1, Slx4, Msh2, Msh6, Mhf1, Mhf2
DNA damaging agents such as nitrogen mustard [1,2],
formaldehyde , and cisplatin  generate many
lesions that inhibit proper DNA replication and tran-
scription. One such lesion, the interstrand crosslink
(ICL), covalently links two complementary DNA strands
and prevents their separation. Importantly, since both
strands are damaged, an undamaged template strand is
not available for repair. Due to these blocks and repair
challenges, ICLs are considered one of the most toxic
DNA lesions. It is estimated that the presence of just
one unrepaired ICL is sufficient to kill yeast or bacteria
 and approximately 40 unrepaired ICLs can kill mam-
malian cells . As a result of this high cytotoxicity,
crosslinking agents are common anticancer agents .
Outside of chemotherapies, ICLs can be induced by
exposures in the environment  and byproducts of nor-
mal metabolic processes [9,10]. Thus, a clearer under-
standing of the mechanisms of ICL repair will inform
our knowledge of both normal and cancer cells. This
article and another recent review  describe novel
findings in yeast that provide insight into the mecha-
nisms of eukaryotic ICL repair.
A yeast fanconi-like pathway emerges
Cells have the capacity to repair ICLs through highly
complex DNA repair mechanisms. ICL repair in the
prokaryotic system is relatively well defined. In Escheri-
chia coli, nucleotide excision repair (NER) creates inci-
sions on each side of the ICL. The resulting short
oligonucleotide is attached through the ICL, but is dis-
placed from the helix, revealing a gap. The gap is filled
in by homologous recombination (HR) or translesion
bypass synthesis (TLS), and the displaced oligonucleo-
tide/ICL adduct is removed by NER .
In lower eukaryotes, defects in most known DNA repair
pathways resultin ICL
eukaryotic mechanisms are much more complex, involve
multiple repair pathways, and can occur in multiple
phases of the cell cycle. Several recent reviews address this
complexity in detail [13-23]. In the budding yeast Sacchar-
omyces cerevisiae, a G1-specific repair pathway involves
NER and TLS similar to the E. coli system . Additio-
nally, three independent epistasis groups (PSO2, RAD52,
and RAD18) are implicated in ICL repair , but each
pathway mechanism is not fully defined. Pso2 is an exo-
nuclease that may be important for cleaving ICL repair
intermediates [26-30]. HR proteins, including Rad52 and
Rad51, likely fill in gaps post-incision and/or repair double
strand breaks (DSBs) that arise during ICL repair. The
post replication repair (PRR) pathway may help fill in the
gaps after the incision and unhooking of ICLs.
In higher eukaryotes the Fanconi anemia (FA) DNA
repair pathway has emerged as a master-regulator of
downstream checkpoints and pathways of ICL repair .
This pathway was named for patients with the heritable,
recessive disorder caused by mutations in FA repair genes.
These mutations confer developmental defects, cancer
* Correspondence: email@example.com
Genome Instability Section, Genetics and Molecular Biology Branch, National
Human Genome Research Institute, National Institutes of Health, 49 Convent
Drive, Bethesda, MD 20892, USA
© 2012 Daee and Myung; licensee BioMed Central Ltd. This is an Open Access article distributed under the terms of the
Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use,
distribution, and reproduction in any medium, provided the original work is properly cited.
Daee and Myung Genome Integrity 2012, 3:7
Figure 1 (See legend on next page.)
Daee and Myung Genome Integrity 2012, 3:7
Page 2 of 5
predisposition, and marked sensitivity to ICL-forming
agents . In the FA repair pathway, FANCM and
FAAP24 are thought to recognize blocked forks, activate
checkpoint responses, and recruit the FA core complex
(FANC A, B, C, E, F, G, L, FAAP100) [32-34]. FANCM is
additionally stabilized by interactions with the MHF1/
MHF2 complex [35,36]. After recruitment, the FA core
complex ubiquitinates FANCD2 and FANCI [32,37].
These ubiquitinated proteins likely promote HR repair
and other poorly understood downstream repair events
mediated by FANCD1, FANCN, FANCP/SLX4, FANCO/
RAD51C and/or FANCJ .
Studies in lower eukaryotic model organisms, like yeasts,
have greatly improved our understanding of most DNA re-
pair pathways. The single-celled yeast model is genetically
tractable and provides a simplistic system for the study of
complex DNA repair problems. Until recently, a yeast FA-
like ICL repair pathway had not been functionally validated.
Mph1, Mhf1/Mhf2, Chl1, and Slx4 are putative homologs
to FANCM, MHF1/MHF2, FANCJ, and FANCP, respect-
ively [34-36,38-41]. Although previous work established
that the yeast proteins Mph1 [42-45], Mhf1/Mhf2 [35,36],
Chl1 [46-48], and Slx4  all play an important role in
maintaining genomic integrity, a role in ICL repair (as indi-
cated by mutant sensitivity to ICL agents) was not appa-
rent. Recent publications from our group  and the
McHugh group  have demonstrated that these proteins
play a previously unappreciated role in ICL repair. Their
function is important for ICL survival when either the Pso2
exonuclease or the PRR helicase Srs2 pathways are inacti-
vated. These studies also revealed roles for additional
proteins in the yeast FA-like pathway including Mgm101,
MutSα (Msh2-Msh6), Exo1, proliferating cell nuclear anti-
gen (Pol30/PCNA), Smc5/6 and Rad5. These studies
provided key mechanistic insights that confirm, clarify, and
bolster our knowledge of the FA pathway, allowing us to
formulate the following model (Figure 1A):
ICL-induced replication stalling recruits or activates
Rad5, which polyubiquitylates PCNA. The helicase Mph1
is recruited to reverse and stabilize the fork. Although
their precise ICL-repair functions are unknown, Chl1,
Mhf1/Mhf2, Smc5/6, and Mgm101 likely help stabilize
Mph1 and/or the ICL repair intermediates. Slx4 may
coordinate incisions surrounding the ICL with its asso-
ciated endonucleases. Also in this pathway, the canonical
mismatch repair complex Msh2-Msh6 (MutSα) potentially
senses the aberrant DNA structure at the fork and/or
recruits Exo1 to digest the tethered ICL-containing oligo-
nucleotide. Oligonucleotide degradation produces a sub-
strate for downstream processing events such as gap-
filling by TLS polymerases or HR. Once the crosslinked
adduct is removed, the DNA replication fork can be
restored. Importantly, this reversed-fork pathway protects
the fragile intermediates of repair (Figure 1B), which can
collapse into double strand breaks and trigger cell death.
The foundational studies by our group and the
McHugh group have validated the yeast FA-like pathway
proteins [50,51]. Despite this, many questions remain
about the precise functions of each protein, particularly
Chl1, Smc5/6, and Mgm101. Chl1 and Smc5/6 have
been implicated in sister chromatid interactions [52-54],
so it is possible that these interactions create a stable
intermediate for engagement by HR. Mgm101 has been
implicated in mitochondrial recombination , so this
role may extend to the nuclear compartment as well. Fu-
ture genetic studies and the examination of ICL repair
intermediates in different mutant backgrounds will
hopefully shed light on these open questions.
In addition to the FA-like ICL repair pathway in yeast,
Pso2 and Srs2 participate in ICL repair. The Pso2 nucle-
ase functions after initial ICL recognition and incision,
which is likely mediated by NER factors . Srs2 is a
helicase that directs the PRR pathway by preventing sub-
strate engagement by recombination proteins [57,58].
Since PRR is a damage tolerance it is not clear how the
ICL is excised through this pathway. It is entirely pos-
sible that, rather than forming independent pathways,
the Pso2- and Srs2-mediated pathways represent the
early (Pso2) and late (PRR) actions of a single pathway.
Mechanistically, these studies confirm the existence of a
yeast ICL repair pathway that is reminiscent of the
mammalian FA pathway. Like the mammalian system
, mismatch repair proteins contribute to the yeast
FA-like pathway. These studies also clarify the contro-
versial role of the PRR pathways [60-62] by demonstrat-
ing that, while the PRR proteins Srs2 and Rad18 are
distinct from the FA pathway, Rad5 and PCNA are
important mediators. Finally, in both yeast [50,51] and
mammalian pathways [35,63], Mph1/FANCM-mediated
(See figure on previous page.)
Figure 1 Model for replication-associated interstrand crosslink repair in yeast. (A) Replication is stalled by an ICL, Rad5 polyubiquitylates
PCNA, and Mph1-mediated fork-reversal stabilizes the fork for repair (with Smc5/6 and Mhf1/2) and protects the repair intermediates from
collapsing into double strand breaks (DSBs). Downstream events of repair are mediated by Slx4 and Exo1. HR and TLS are important for gap-
filling steps. The figure key shows the putative human homologs in brackets. (B) The basic steps of ICL repair lead to various fragile intermediates
(ssDNA, single strand DNA) that can collapse into DSBs. Cell death is triggered if the DSB cannot be repaired.
Daee and Myung Genome Integrity 2012, 3:7
Page 3 of 5
fork regression or stabilization likely protects ICL repair
intermediates from inappropriate processing or repair.
Despite the presence of a large core complex in the
mammalian FA repair pathway, the yeast pathway appears
to be substantially stripped down. It remains to be seen
whether a core-like complex will be identified in yeast or
whether evolutionary divergence was sparked by the need
for the large complex in mammals. Furthermore, since the
mammalian FA pathway appears to be a master regulator
of repair it is surprising that the yeast pathway is secon-
dary to Pso2- or Srs2-mediated events. Despite these dif-
ferences, the simplified yeast model offers significant
advantages for the FA repair field to address fundamental
mechanistic questions in the future.
ICL: Interstrand crosslink; TLS: Translesion synthesis; NER: Nucleotide excision
repair; HR: Homologous recombination; PRR: Postreplication repair;
FA: Fanconi anemia; ssDNA: Single strand DNA; DSB: Double strand break.
The authors declare no competing interests with the contents of this
The manuscript was prepared by D.L.D with editorial and substantive advice
from K.M. Both authors read and approved the final manuscript.
We thank members in Myung laboratory for helpful discussions and
comments on the manuscript; and K.M. especially thanks E. Cho. This
research was supported by the Intramural Research Programs of the National
Human Genome Research Institute to KM. We apologize to researchers
whose studies we could not discuss or cite due to space limitations.
Received: 21 August 2012 Accepted: 9 October 2012
Published: 12 October 2012
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Cite this article as: Daee and Myung: Fanconi-like crosslink repair in
yeast. Genome Integrity 2012 3:7.
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