Ultraviolet absorbance and circular dichroism of Pf1 virus: nucleotide/subunit ratio of unity, hyperchromic tyrosines and DNA bases, and high helicity in the subunits.
Ultraviolet absorbance and circular dichroism of Pf1 virus: nucleotide/subunit ratio of unity, hyperchromic tyrosines and DNA bases, and high helicity in the subunits.
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Pf1病毒的紫外吸光度和圆二色性：核苷酸/亚基比例一致，酪氨酸和DNA碱基增色，亚基中的螺旋度高。
DOI：
10.1021/bi00173a011
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发表时间：
1994
期刊：
影响因子：
2.9
通讯作者：
Day,LA
中科院分区：
文献类型：
--
作者：
Kostrikis,LG;Liu,DJ;Day,LA
摘要：已经获得了Pfl病毒的化学计量学数据，并确定了其DNA和蛋白质的结构特征。解离病毒在碱性变性条件下的吸光度光谱与DNA和蛋白质在每个蛋白质亚基一个核苷酸的摩尔比下的光谱完全吻合。该结果与之前三个独立方法的结果一致，确定了Pfl的核苷酸/亚基比（n/s）是统一的。完整原生病毒DNA的吸光度谱与热变性Pfl DNA的吸光度谱相同，在259 nm处<(P)= 8400 M"* 1 cm-1。完整病毒中蛋白质（两个酪氨酸）的吸光度谱在Xmax为281.5 nm时< e (Y))= 2500 M_l cm" 1 /酪氨酸；这是已知的最红移和高变色的酪氨酸光谱。完整病毒在250 ~ 320 nm的CD谱中没有明显的DNA贡献，但红移酪氨酸的贡献很大。185 ~ 250 nm范围内的CD光谱具有a-螺旋CD参考光谱的形状，但明显存在蓝移，在199.7 nm处具有从负椭圆到正椭圆的交叉，并且具有非常高的振幅（例如[02O7]）。5nm]=- 44000°cm2 dmol1)。该谱显示病毒蛋白完全呈螺旋状，以a-螺旋结构为主，可能有3| - o-螺旋结构。单位n/s比、DNA碱基的高吸光度和可忽略的双紫外CD以及螺旋蛋白的高振幅是确定Pfl病毒结构的关键输入数据。感染铜绿假单胞菌K株的Pfl病毒是所有已知丝状病毒中最长的（Takeya & Amako, 1966; Bradley, 1973）。图1显示了单个病毒粒子的电子显微镜照片，显示了它的极长（2000纳米）和小直径（小于7纳米），以及DNA和蛋白质的关系图。7349个核苷酸的拓扑环状单链基因组（Hill et al., 1991）从病毒粒子的一端延伸到另一端，然后再延伸回来，形成两条反平行链
Revised Manuscript Received November 30, 1993® abstract: Data have been obtained for the Pfl virionthat establish its stoichiometry and conformational features of its DNA and its protein. The absorbance spectrum of the dissociated virus under alkaline denaturing conditions is fit exactly by spectra for DNA and protein at a mole ratio of one nucleotide per protein subunit. This result, together with three previous values by independent methods, establishes that the nucleotide/subunit ratio (n/s) of Pfl is unity. Theabsorbance spectrum of DNA in the intact native virus is assigned as the spectrum for heat denatured Pfl DNA, with<(P)= 8400 M"* 1 cm-1 at 259 nm. The absorbance spectrum assigned to protein (two tyrosines) in the intact virus has< e (Y))= 2500 M_l cm" 1 per tyrosine at Xmax of 281.5 nm; this is the most red-shifted and hyperchromic tyrosine spectrum known. The CD spectrum of the intact virus from 250 to 320 nm has no apparent DNA contribution, but has a strong contribution from the red-shifted tyrosine (s). The CD spectrum from 185 to 250 nm has the shape of a-helical CD reference spectra, but is perceptibly blue-shifted, with a crossover from negative to positive ellipticity at 199.7 nm, and it has very high amplitudes (eg [02O7. 5nm]=-44 000 deg cm2 dmol1). This spectrum indicates completely helical protein in the virus, with a predominance of a-helix and perhaps some 3| o-helix. The unit n/s ratio, the high absorbance and negligiblenear-UV CD for the DNA bases, and the high amplitudes for the helical protein are critical input data for the determination of Pfl virus structure.Pfl virus, which infects Pseudomonas aeruginosa strain K, is the longest of allknown filamentous viruses (Takeya & Amako, 1966; Bradley, 1973). An electron micrograph of a single virion, displaying itsextreme length (2000 nm) and small diameter (less than 7 nm), is shownin Figure 1, together with a diagram of the relation of the DNA and protein. The topologically circular single-stranded genome of 7349 nu-cleotides (Hill et al., 1991) extends from one end of the virion to the other and back again, forming two antiparallel strands
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