[Frontiers in Bioscience 11, 3062 -3080, September 1, 2006]

MutY and MutY homologs (MYH) in genome maintenance

A-Lien Lu, Haibo Bai, Guoli Shi, and Dau-Yin Chang

Department of Biochemistry and Molecular Biology, University of Maryland, Baltimore, Maryland

TABLES

Table 1. 8-oxoG Repair Enzymes in Different Organisms

E. coli

Human

S. cerevisiae

S. pombe

Bacteria

Mammal

Baking yeast

Fission yeast

MutY

hMYH

No

SpMYH

MutT

hMTH1

ScMTH1

?

MutM

hOGG1

ScOGG1

No

 

hOGG2

ScOGG2

 

MutS

hMSH2/MSH6

ScMSH2/hMSH6

SpMSH2/MSH6

 

hMSH2/MSH3

ScMSH2/MSH3

SpMSH2/MSH3

 

Others

Others

Others

Nei (EndoVIII)

hNEIL1

No

No

 

hNEIL2

 

 

 

hNEIL3

 

 

This table is reproduced from Lu (169) with permission from Elsevier.

Table 2. Apparent Dissociation Constants (Kd) of E. coli MutY

DNA duplex

Kd (nM)

A/G-20

5.3 ± 0.5b

A/C-20

15 ± 3b

A/GO-20

0.07 ± 0.01b

AP/G-20

2.2 ± 0.3b

AP/GO-20

0.18 ± 0.11c

C/GO-20

11.5 ± 3.8c

T/GO-20

0.11 ± 0.01c

G/GO-20

0.11 ± 0.01b

A/G-44

1.8 ± 0.3b

A/GO-44

0.14 ± 0.01d

C:G-20

375 ± 80b

C:G-44

315 ± 49d

A/hoU

124 ± 14e

a The mismatched duplex DNA substrates are represented by a base-base mismatch followed by the chain length (number of base pairs). C:G represents a homoduplex DNA substrate. Dissociation constants for E. coli MutY are derived from references 57b, 80c, 114d, and 29e. This table is adapted from Lu (169) with permission from Elsevier.