The MutL ATPase Is Required for Mismatch Repair

Spampinato, Claudia P.; Modrich, Paul

doi:10.1074/jbc.275.13.9863

Cited by 118 publications

(91 citation statements)

References 36 publications

(22 reference statements)

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“…Thus, stimulation of the UvrD-catalyzed unwinding reaction by MutL is specific and likely due to a protein-protein interaction. This is consistent with data demonstrating a physical interaction between these two proteins (25,26).…”

supporting

confidence: 82%

“…1A). This finding suggests that, although MutL and UvrD are known to physically interact (25,26), stimulation of the UvrD-catalyzed unwinding reaction is also related to the ability of MutL to bind DNA. Since the fraction of the substrate unwound is directly related to the amount of UvrD productively pre-bound to DNA, it follows that MutL increases the affinity of UvrD for a partial duplex substrate.…”

Section: Resultsmentioning

confidence: 81%

“…It is likely that the supershifted species is due to the specific interaction between MutL and UvrD, and not to UvrD and MutL independently binding to the ssDNA for the following reasons. MutL and UvrD physically interact both in vitro (in the absence of DNA) and in vivo (25,26). In addition, in the presence of MutL ϩ UvrD, there was a complete absence of the DNA species associated with MutL alone (compare lanes 2 with lanes 3 and 5), indicating that MutL prefers to bind to UvrD⅐DNA.…”

Section: Resultsmentioning

confidence: 90%

“…A physical interaction between these proteins has been demonstrated (25,27), and MutL greatly stimulates the unwinding activity of UvrD (27,29). Based on the results presented here, we propose that MutL loads UvrD productively onto the DNA, but does not clamp UvrD onto the DNA during the unwinding reaction.…”

Section: Discussionmentioning

confidence: 90%

“…Some groups have demonstrated that MutL binds to both ssDNA and double-stranded DNA (21,22), whereas others have reported that MutL does not bind DNA (23). It is now clear that MutL catalyzes a weak ATPase reaction and that this activity is required for mismatch repair (21,24,25). In addition, MutL stimulates the biochemical activities of MutS, MutH, and helicase II (12, 13, 23, 24, 26 -29), and several lines of evidence indicate there is a physical interaction between MutL and MutS (12,13,23), MutL and MutH, and MutL and helicase II (26,27).…”

mentioning

confidence: 99%

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Escherichia coli MutL Loads DNA Helicase II onto DNA

Mechanic¹,

Frankel²,

Matson³

2000

Journal of Biological Chemistry

116

119

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supporting

confidence: 82%

Section: Resultsmentioning

confidence: 81%

Section: Resultsmentioning

confidence: 90%

Section: Discussionmentioning

confidence: 90%

mentioning

confidence: 99%

See 3 more Smart Citations

Escherichia coli MutL Loads DNA Helicase II onto DNA

Mechanic¹,

Frankel²,

Matson³

2000

Journal of Biological Chemistry

116

119

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A whole new way of looking at things: The use of Dark Reader technology to detect fluorophors

Seville

2001

Electrophoresis

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The Dark Reader optical system (Clare Chemical Research, Denver, CO, USA) uses relatively low intensity broad-band visible blue light in combination with broad-band optical filters to detect fluorescence with a level of sensitivity that often surpasses that of UV transilluminators and can rival that of laser-based scanners. Applications of DR (Clare Chemical Research) devices include the detection of DNA and SYBR-stained protein samples following, and also during, electrophoresis. Unlike laser-based imaging systems, the fluorescence is directly visible to the user as well as being fully compatible with charge-coupled device (CCD) and Polaroid camera-based detection and imaging. Additionally, the DR optical system functions well in multicolor fluorophor environments. Because the Dark Reader does not emit any UV light, the extent of DNA damage incurred when visualizing DNA samples is drastically reduced compared to the damage produced by a UV device and this can have a significant benefit on downstream cloning protocols. Furthermore, dye photobleaching is minimal, extending the length of time that a fluorescent sample is visible. The inherent flexibility of the DR optical system allows many different configurations of the Dark Reader to be constructed such as transilluminators, hand lamps and integrated transilluminator-electrophoresis units.

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MutL: conducting the cell's response to mismatched and misaligned DNA

Polosina

Cupples

2009

BioEssays

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Base pair mismatches in DNA arise from errors in DNA replication, recombination, and biochemical modification of bases. Mismatches are inherently transient. They are resolved passively by DNA replication, or actively by enzymatic removal and resynthesis of one of the bases. The first step in removal is recognition of strand discontinuity by one of the MutS proteins. Mismatches arising from errors in DNA replication are repaired in favor of the base on the template strand, but other mismatches trigger base excision or nucleotide excision repair (NER), or non-repair pathways such as hypermutation, cell cycle arrest, or apoptosis. We argue that MutL homologues play a key role in determining biologic outcome by recruiting and/or activating effector proteins in response to lesion recognition by MutS. We suggest that the process is regulated by conformational changes in MutL caused by cycles of ATP binding and hydrolysis, and by physiologic changes which influence effector availability.

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The MutL ATPase Is Required for Mismatch Repair

Abstract: Members of the

Cited by 118 publications

References 36 publications

Escherichia coli MutL Loads DNA Helicase II onto DNA

Escherichia coli MutL Loads DNA Helicase II onto DNA

A whole new way of looking at things: The use of Dark Reader technology to detect fluorophors

MutL: conducting the cell's response to mismatched and misaligned DNA

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