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Nucleotide, protection

Fig. 4.4 Secondary structure of the PTC and antibiotic information. Nucleotide numbering is from H. marismortui (Hm) and is followed by the standard corresponding coli (Ec) numbering in parentheses. Nucleotides with superscripts have been implicated in antibiotic interactions by nucleotide protection studies (green) [54-57] or by mutations (orange) that confer resistance to carbomycin A (M) linco-samides (L) streptogramin A [58] (S) chlor-... Fig. 4.4 Secondary structure of the PTC and antibiotic information. Nucleotide numbering is from H. marismortui (Hm) and is followed by the standard corresponding coli (Ec) numbering in parentheses. Nucleotides with superscripts have been implicated in antibiotic interactions by nucleotide protection studies (green) [54-57] or by mutations (orange) that confer resistance to carbomycin A (M) linco-samides (L) streptogramin A [58] (S) chlor-...
Currently, one structure of a Irncosamide antibiotic bound to the ribosome is available for analysis [4]. like the macrolide antibiotics, drndamycin binds near the hydrophobic crevice at the entrance to the peptide exit turmel. As with the macrolide carbomycin A, dindamycin interacts not only with the hydrophobic crevice at the entrance to the peptide exit turmd, but also with the active site hydrophobic crevice. The nudeotides that surroimd the clindamydn binding site were previously implicated in binding of lincosamides based on nucleotide protection studies and on the analysis of mutations conferred by resistance (Fig. 4.4). [Pg.114]

Two crystal structures of chloramphenicol bound to the ribosome are available. In one structure, chloramphenicol is observed to bind only at the active site hydro-phobic crevice of the bacterial (D. radiodurans) ribosome [4]. In the other structure chloramphenicol binds only at the hydrophobic crevice at the entrance to the exit tunnel of an archaeal (H. marismortui) ribosome [7]. Both of these sites are surrounded by nucleotides implicated in chloramphenicol binding either by nucleotide protection studies or by mutational studies (Fig. 4.12). They probably correspond to the two sites inferred from biochemical experiments. [Pg.116]

BP-Phe-tRNA crosslink P site bound BP-Phe-tRNA crosslink A site bound azidopuromycin crosslink nucleotides protected by tRNA bound to A site P site... [Pg.445]

Fig. 2. The peptidyltransferase center. The structure of the central loop of Domain V of E. coli 23S rRNA is shown. Nucleotides involved in resistance against different inhibitors are indicated. Closed symbols indicate resistance and open symbols protection against chemical modification by bound antibiotic. Mutations that confer resistance to anisomycin in archaea are indicated [87] (Hcu, Halobacterium cutirubrum Hha, H. halobium). The presence of either a G or U at position 2058 in archaea is also indicated. As a consequence of this change archaea are resistant to erythromycin (Hmo, Halococcus morrhuae, Mva, Methanococcus vannielii Tte, Thermoproteus lenax Dmo, Desulfurococcus wofirfo) [29,30,88,90]. Positions where crosslinking to photoreactive derivatives of Phe-tRNA and puromycin have been observed as well as nucleotides protected by bound tRNA are also indicated. Modified from ref [73]. Fig. 2. The peptidyltransferase center. The structure of the central loop of Domain V of E. coli 23S rRNA is shown. Nucleotides involved in resistance against different inhibitors are indicated. Closed symbols indicate resistance and open symbols protection against chemical modification by bound antibiotic. Mutations that confer resistance to anisomycin in archaea are indicated [87] (Hcu, Halobacterium cutirubrum Hha, H. halobium). The presence of either a G or U at position 2058 in archaea is also indicated. As a consequence of this change archaea are resistant to erythromycin (Hmo, Halococcus morrhuae, Mva, Methanococcus vannielii Tte, Thermoproteus lenax Dmo, Desulfurococcus wofirfo) [29,30,88,90]. Positions where crosslinking to photoreactive derivatives of Phe-tRNA and puromycin have been observed as well as nucleotides protected by bound tRNA are also indicated. Modified from ref [73].
Fig. 1. Secondary structure model for the 5 end of STNV RNA. The model depicts stable secondary interactions, based on sequence (Ysebaert et al., 1980) and prominent sites of ribonuclease Ti cleavage (arrows Kaempfer et al., 1981). (Line) nucleotides protected by 40 S ribosomal subunits against nucleases (Browning et al., 1980). For eIF-2-binding site, see text. From Kaempfer et al., 1981. Fig. 1. Secondary structure model for the 5 end of STNV RNA. The model depicts stable secondary interactions, based on sequence (Ysebaert et al., 1980) and prominent sites of ribonuclease Ti cleavage (arrows Kaempfer et al., 1981). (Line) nucleotides protected by 40 S ribosomal subunits against nucleases (Browning et al., 1980). For eIF-2-binding site, see text. From Kaempfer et al., 1981.
This indicates that this effect is probably not due to a post illumination ATP formation. Similar results were obtained with freshly broken and washed chloroplasts (light activated with PMS + DTT). As has been shown before. Pi, PPi, ATP and other nucleotides protect against ADP induced deactivation. [Pg.530]

Trichloro- and 2,2,2-tribromoethoxycarbonyl (Tceoc and Tbeoc) protecting groups are introduced with the commercially available 2,2,2-trihaloethyl chloroformates. These derivatives are stable towards CrOj and acids, but can smoothly be cleaved by reduction with zinc in acetic acid at 20 °C to yield 1,1-dihaloethene and CO. Several examples in lipid (F.R. Pfeiffer, 1968, 1970) and nucleotide syntheses (A.F. Cook, 1968) have been described. [Pg.158]

The benzyl group has been widely used for the protection of hydroxyl functions in carbohydrate and nucleotide chemistry (C.M. McCloskey, 1957 C.B. Reese, 1965 B.E. Griffin, 1966). A common benzylation procedure involves heating with neat benzyl chloride and strong bases. A milder procedure is the reaction in DMF solution at room temperatiue with the aid of silver oxide (E. Reinefeld, 1971). Benzyl ethers are not affected by hydroxides and are stable towards oxidants (e.g. periodate, lead tetraacetate), LiAIH, amd weak acids. They are, however, readily cleaved in neutral solution at room temperature by palladium-catalyzed bydrogenolysis (S. Tejima, 1963) or by sodium in liquid ammonia or alcohols (E.J. Rcist, 1964). [Pg.158]

Table 19. Protecting groups used for nucleotides (see also section 2.6.). Table 19. Protecting groups used for nucleotides (see also section 2.6.).
Ethers are among the most used protective groups in organic synthesis. They vary from the simplest, most robust, methyl ether to the more elaborate, substituted, trityl ethers developed for use in nucleotide synthesis. They are formed and removed under a wide variety of conditions. Some of the ethers that have been used to protect alcohols are included in Reactivity Chart 1. ... [Pg.14]

Ph2CHC02-2-tetrahydrofuranyl, 1% TsOH, CCI4, 20°, 30 min, 90-99% yield. The authors report that formation of the THF ether by reaction with 2-chlorotetrahydrofuran avoids a laborious proce ure that is required when dihydrofuran is used. In addition, the use of dihydrofuran to protect the 2 -OH of a nucleotide gives low yields (24-42%)." The tetrahydrofuranyl ester is reported to be a readily available, stable solid. A tetrahydrofuranyl ether can be cleaved in the presence of a THP ether. ... [Pg.36]

These were originally prepared by Khorana as selective protective groups for the 5 -OH of nucleosides and nucleotides. They were designed to be more acid-labile than the trityl group because depurination is often a problem in the acid-catalyzed removal of the trityl group. Introduction of p-methoxy groups increases the rate of hydrolysis by about one order of magnitude for each p-methoxy substituent. For 5 -protected uridine derivatives in 80% AcOH, 20°, the time for hydrolysis was... [Pg.62]

The consequence of ADA deficiency is accumulation of adenosine and 2 -deoxyadenosine, substances toxic to lymphocytes, important cells in the immune response. 2 -Deoxyadenosine is particularly toxic because its presence leads to accumulation of its nucleotide form, dATP, an essential substrate in DNA synthesis. Elevated levels of dATP actually block DNA replication and cell division by inhibiting synthesis of the other deoxynncleoside 5 -triphosphates (see Chapter 27). Accumulation of dATP also leads to selective depletion of cellular ATP, robbing cells of energy. Children with ADA SCID fail to develop normal immune responses and are susceptible to fatal infections, unless kept in protective isolation. [Pg.420]

This is a fluorescent benzyl ether used for 2 -protection in nucleotide synthesis. It is introduced using 1 -pyrenylmethyl chloride (KOH, benzene, dioxane, reflux, 2 h, >65% yield). Most methods used for benzyl ether cleavage should be applicable to this ether. [Pg.100]

A nitrophenylsulfenate, cleaved by nucleophiles under very mild conditions, was developed as protection for a hydroxyl group during solid-phase nucleotide synthesis. The sulfenate ester is stable to the acidic hydrolysis of acetonides. ... [Pg.196]

A great many protective groups have been developed for the amino group, including carbamates (>NC02R), used for the protection of amino acids in peptide and protein syntheses, and amides (>NCOR), used more vv idely in syntheses of alkaloids and for the protection of the nitrogen bases adenine, cytosine, and guanine in nucleotide syntheses. [Pg.502]

All the approaches for deblocking protective groups described earlier in this book have found application in the removal of protective groups from phosphorus derivatives. Because phosphate protection and deprotection are commonly associated with compounds that contain acid-sensitive sites (e.g., glycosidic linkages and DMTr-O- groups of nucleotides), the most widely used protective groups on phosphorus are those that are deblocked by base. [Pg.666]

DNA synthesizers operate on a principle similar to that of the Merrifield solid-phase peptide synthesizer (Section 26.8). In essence, a protected nucleotide is covalently bonded to a solid support, and one nucleotide at a time is added to the growing chain by the use of a coupling reagent. After the final nucleotide has been added, all the protecting groups are removed and the synthetic DNA is cleaved from the solid support. Five steps are needed ... [Pg.1114]

Although the 3 - and 5 -polyphosphate derivatives mentioned above exhibit exquisite inhibitory potency these compounds are not cell permeable. To take advantage ofthepotency of such derivatives for studies with intact cells and tissues, there are two possibilities. One is chemically to protect the phosphate groups from exonucleotidases that also allows the compound to transit the membrane intact. The other is to provide a precursor molecule that is cell permeable and is then metabolized into an inhibitor by intracellular enzymes. The general term for such a compound is prodrug nucleotide precursors are also referred to as pronucleotides. Families of protected monophosphate derivatives were synthesized, based on (3-L- and 3-D-2, 5 -dd-3 -AMP, 3-L-2, 3 -dd-5 -AMP, and the acyclic 9-substituted adenines, PMEA and PMPA. Protective substituents were (i) -( -pivaloyl-2-thioethyl) ... [Pg.36]

RNAse is an enzyme that catalyses the breakdown of RNA molecules into their component nucleotides. RNAses are extremely common in the modern world, resulting in very short life spans for any RNA that is not in a protected environment. [Pg.1094]


See other pages where Nucleotide, protection is mentioned: [Pg.115]    [Pg.489]    [Pg.88]    [Pg.538]    [Pg.115]    [Pg.489]    [Pg.88]    [Pg.538]    [Pg.112]    [Pg.154]    [Pg.217]    [Pg.341]    [Pg.258]    [Pg.259]    [Pg.492]    [Pg.80]    [Pg.116]    [Pg.349]    [Pg.49]    [Pg.333]    [Pg.382]    [Pg.382]    [Pg.23]    [Pg.105]    [Pg.550]    [Pg.66]    [Pg.1114]    [Pg.32]    [Pg.336]   
See also in sourсe #XX -- [ Pg.96 ]




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