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首页> 外文期刊>Biochemistry >Demonstration by ultraviolet resonance Raman spectroscopy of differences in DNA organization and interactions in filamentous viruses Pf1 and fd.
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Demonstration by ultraviolet resonance Raman spectroscopy of differences in DNA organization and interactions in filamentous viruses Pf1 and fd.

机译：通过紫外线共振拉曼光谱论证了丝状病毒Pf1和fd中DNA组织和相互作用的差异。

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Pf1, a class II filamentous virus, has been investigated by ultraviolet resonance Raman (UVRR) spectroscopy with excitation wavelengths of 257, 244, 238, and 229 nm. The 257-nm UVRR spectrum is rich in Raman bands of the packaged single-stranded DNA (ssDNA) genome, despite the low DNA mass (6%) of the virion. Conversely, the 229-nm UVRR spectrum is dominated by tyrosines (Tyr 25 and Tyr 40) of the 46-residue alpha-helical coat subunit. UVRR spectra excited at 244 and 238 nm exhibit Raman bands diagnostic of both viral DNA and coat protein tyrosines. Raman markers of packaged Pf1 DNA contrast sharply with those of the DNA packaged in the class I filamentous virus fd [Wen, Z. Q., Overman, S. A., and Thomas, G. J., Jr. (1997) Biochemistry 36, 7810-7820]. Interestingly, deoxynucleotides of Pf1 DNA exhibit sugars in the C2'-endo/anti conformation and bases that are largely unstacked, compared with C3'-endo/anti conformers and very strong base stacking in fd DNA; hydrogen-bonding interactions of thymine carbonyls are also different in Pf1 and fd. On the other hand, coat protein tyrosines of Pf1 exhibit Raman markers of ring environment identical to those of fd, including an anomalous singlet at 853 cm-1 in lieu of the canonical Fermi doublet (850/830 cm-1) found in globular proteins. The results indicate markedly different modes of organization of ssDNA in Pf1 and fd virions, despite similar environments for coat protein tyrosines, and suggest strong hydrogen-bonding interactions between DNA bases and coat subunits of Pf1 but not between those of fd. We propose that structural relationships between the protein coat and encapsidated ssDNA genome are also fundamentally different in the two assemblies.
机译：Pf1是一种II类丝状病毒，已通过紫外共振拉曼（UVRR）光谱研究，激发波长为257、244、238和229 nm。尽管病毒体的DNA质量较低（6％），但257 nm的UVRR光谱富含已包装的单链DNA（ssDNA）基因组的拉曼带。相反，229 nm UVRR光谱由46个残基的α-螺旋涂层亚基的酪氨酸（Tyr 25和Tyr 40）主导。在244和238 nm处激发的UVRR光谱对病毒DNA和外壳蛋白酪氨酸都有拉曼谱带诊断。包装的Pf1 DNA的拉曼标记与包装在I类丝状病毒fd中的DNA的拉曼标记形成鲜明对比[Wen，Z.Q.，Overman，S.A。，和Thomas，G.J.，Jr。（1997）Biochemistry 36，7810-7820]。有趣的是，与C3'-endo / anti构象和fd DNA中非常强的碱基堆积相比，Pf1 DNA的脱氧核苷酸在C2'-endo / anti构象中显示糖，并且大部分碱基没有堆叠。胸腺嘧啶羰基的氢键相互作用在Pf1和fd中也不同。另一方面，Pf1的外壳蛋白酪氨酸表现出与fd相同的环环境拉曼标记，包括在853 cm-1处出现异常单重态来代替在球状蛋白质中发现的经典费米二重态（850/830 cm-1） 。结果表明，尽管外壳蛋白酪氨酸具有相似的环境，但在Pf1和fd病毒体中ssDNA的组织模式显着不同，并且表明DNA碱基与Pf1的外壳亚基之间存在强烈的氢键相互作用，但在fd的DNA碱基与外壳亚基之间却没有强相互作用。我们建议蛋白质外壳和衣壳化的ssDNA基因组之间的结构关系在两个程序集中也根本不同。

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