Deletion duplex

Figure 10.7 Proposed translesion synthesis for Norl-induced -2 deletion mutations. Incorporation of correct dC opposite dG-C8-FAF and subsequent nucleotide incorporation (e.g., dC) can lead to formation of stable S- and B-conformer SMIs (S-SMI and B-SMI, respectively), (a) Sequences for Norl-dC/-2 and Norl-dT/-2 deletion duplexes, (b) The Norl-dC/-2...

Fig. 6. A field of T7 heads obtained from a cryoelectron micrograph of a complete tail-deletion (genes 11 and 12) mutant. Empty capsids appear as thin-walled particles. Full capsids exhibit the characteristic 2.5-nm spacing of densely packed DNA duplexes in motifs that vary according to viewing direction. The concentric ring motif is discemable in the views along the axis that passes through the connector-core vertex that is in the center of the particle.

Cosman, M., Fiala, R., Hingerty, B.E., Amin, S., Geacintov, N.E., Broyde, S., and Patel, D.J. (1994) Solution conformation of the (+)-cis-anti-[BP]dG adduct opposite a deletion site in a DNA duplex intercalation of the covalently attached benzojajpyrene into the helix with base displacement of the modified deoxyguanosine into the minor groove. Biochemistry, 33, 11518-11527. 

Two independently-folding domains. A variety of methods were applied to examine the structure of intact hairpin ribozymes, ribozyme-substrate complexes, and ribozyme derivatives in which some sequences were deleted. Crosslinking studies, gel mobility analysis, and chemical modification experiments suggested that the ribozyme consists of two independently-folding domains. Domain A is a duplex between the substrate and substrate-binding strand (helix 1, loop A and helix 2), while domain B consists of helix 3, loop B and helix 4. 

DNA damage includes DNA polymerase errors (deletion or insertion of bases), strand breaks caused by X-rays, and cross-linking (e.g. psoralen) between duplex strands that prevents strand separation, e.g. thymine cross-linking across the duplex. 

Hin DNA invertase has been sequenced and X-ray studies have been performed on the protein on its complexes with DNA. It consists of a 52-residue C-terminal DNA-binding domain and a 138-bp catalytic domain. yS-Resolvase (a dimer of identical 120-resi-due subunits encoded by the y5 transposon) displays 40 % sequence identity with the Hin catalytic domain, and catalyses a similar reaction, i.e. a 2-bp staggered cleavage, exchange, and re-ligation of duplex DNA. Whereas Hin catalyses an inversion, y8 resolvase catalyses a site-specific deletion. 

Each cellular licensee in a MSA or RSA is authorized by the FCC to use 25 MHz of spectrum within the 800-MHz range. Originally, the FCC allocated 20 MHz to each carrier, which was obtained by deleting UHF television channels 70-83 because they were lightly used. An additional 5 MHz per carrier was authorized in 1985 due to growing capacity problems in some areas. This 25 MHz of spectrum is divided for use by base and mobile stations within each system so that different frequencies are used for base-to-mobUe and mobile-to-base. This type of operation is called full duplex and permits simultaneous conversation or transmission. It must be remembered that two channels are required for each conversation in order to operate on a full-duplex basis. 

Another efficient strategy for generating unidirectional deletions exploits the resistance of a-thiophosphate-containing phosphodiester bonds to the 3 — 5 -exonuclease activity of T4 DNA Pol (57). In this strategy, the 3 terminus of a linearized, duplex plasmid DNA is filled in with dNMPaS by using E. coli DNA Pol Ik. The other end of the target sequence is then cleaved at an appropriate... 

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