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E. coli, recognizes uracil within DNA and cleaves it out at the base-sugar (glycosidic) bond. The resulting site is called an AP (apurinic-apyrimidinic) site, because of the lack of a purine or pyrimidine at the site (see g. 12.23). An AP endonuclease then senses the minor distortion of the DNA double helix and initiaties excision of the single AP nucleotide in a process known as base excision repair. The AP endonuclease nicks the DNA at the 5 side of the base-free AP site. A DNA polymerase then inserts a nucleotide at the AP site; an exonuclease, lyase, or phosphodiesterase enzyme then removes the base-free nucleotide. (Lyases are enzymes that can break C-C, C-O, and C-N bonds.) DNA ligase then closes the nick ( g. 12.29). The replacement of just one base occurs 80 90% of the time. In the remaining 10 20% of cases, several nucleotides may be removed, depending probably on which DNA polymerase (I or III) first repairs the site (fig. 12.29). In mammals, DNA polymerase performs two roles in base excision repair: It both inserts a new base where the AP site was and also eliminates the AP nucleotide residue by exonuclease activity. One question that concerned scientists was how the glycosylases gain access to the inappropriate or damaged bases within the double helix. Recently, it has been demonstrated that these enzymes remove the inappropriate or damaged bases by rst ipping them out of the interior of the double helix in a process called base ipping. For example, the enzyme in human beings that recognizes 8-oxoguanine in DNA (see fig. 12.19), 8-oxoguanine DNA glycosylase, ips the base out to excise it. Base ipping seems to be a common mechanism in repair enzymes that need access to bases within the double helix ( g. 12.30).

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Fig 410: SEM micrographs of the bondless diamond wheel surface: (a) a thermally treated wheel, (b) a chemically

Table 92 Regions of operation and equations of n-channel depletion MOSFET and of JFET Cutoff region: vGS < VP Ohmic or triode region: vDS < 025(vGS + VP ), vGS > VP 2 VP (equivalent drain-to-source resistance) RDS = 2IDSS (vGS + VP ) vDS iD RDS Saturation region: vDS vGS + VP , vGS > VP IDSS (vGS + VP )2 2 VP Breakdown region: vDS > VB iD =

80 90%

Known Quantities: Drain resistance; JFET parameters IDSS and VP Find: Operating region of each JFET

Schematics, Diagrams, Circuits, and Given Data: VDD = 15 V; RD(a) = 500 Assumptions: Use the JFET equations of Table 92 Analysis:

10 20%

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1 Circuit (a) Since vGS = 0, we know (by de nition) that iD = IDSS = 10 mA We can therefore write the drain circuit equation: VDD = RD iD + vDS and calculate vDS = VDD RD iD = 15 500 10 2 = 10 V From Table 92, we see that the condition for operation in the saturation region is vDS > VGS + VP Since 10 > 0 + 4, we conclude that the JFET of circuit (a) is operating in the active region 2 Circuit (b) The drain circuit equation is: VDD = RD iD + vDS and vDS = VDD RD iD = 15 145 103 10 2 = 05 V From Table 92, we see that the condition for operation in the saturation region is vDS > vGS + VP , but in this case, 05 < 0 + 4, and we therefore conclude that the JFET is in the ohmic region We can also directly check the condition for ohmic operation given in Table 92: |vDS | < 025(vGS + VP ) and con rm that, indeed, the JFET operates in the ohmic region since 05 < 1

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treated wheel and (c) a chemically treated wheel with cauliflower-like facets [27]

Whereas base excision repair is initiated by glycosylases and usually involves the replacement of only one nucleotide residue, nucleotide excision repair is initiated by enzymes that sense distortions in the DNA backbone and replace a short stretch of nucleotides. For example, six enzymes in E. coli excise a short stretch of DNA containing thymine dimers if the dimerization is not reversed by photoreactivation. Two copies of the protein product of the uvrA gene (for ultraviolet light UV repair) combine with one copy of the product of the uvrB gene to form a UvrA2UvrB complex that moves along the DNA, looking for damage ( g. 12.31). (The complex has 5 to 3 helicase activity.) When the complex nds damage such as a thymine dimer, with moderate to large distortion of the DNA double helix, the UvrA2 dimer dissociates, leaving the UvrB subunit alone. This causes the DNA to bend and attracts the protein product of the uvrC gene, UvrC. The UvrB subunit rst

Design the JFET bias circuit of Figure 943 to operate in the saturation region with a drain current of 4 mA and a drain-source voltage of 10 V

Figure 12.29 Mechanism of base excision repair. In this case,

Schematics, Diagrams, Circuits, and Given Data: VP = 3 V; IDSS = 6 mA; iDQ = 4 Assumptions: Use the JFET equations of Table 92

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