Reactivity of the tyrosine residues of tobacco mosaic virus protein with iodine

Fraenkel‐Conrat, H.; Sherwood, Marie T.

doi:10.1016/0003-9861(67)90520-6

Cited by 24 publications

(5 citation statements)

References 12 publications

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“…However, this picture requires, in addition, that all three tryptophan residues (17, 52, and 152), widely separated on the polypeptide chain, be at the surface of a subunit and near the RNA coil. Besides being a very stringent constraint for the architecture of TMV particles, the requirement disagrees with the finding that the residues 138-158 are comparatively peripheral on the virus particle (Anderer et al, 1965; Harris and Knight, , 1955Fraenkel-Conrat and Colloms, 1967;Fraenkel-Conrat and Sherwood, 1967). Therefore, we do not favor this possibility.…”

Section: Resultscontrasting

confidence: 73%

Optical rotatory dispersion, tryptophan location, and base distribution in tobacco mosaic virus

Cheng¹

1968

Biochemistry

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Section: Resultscontrasting

confidence: 73%

Optical rotatory dispersion, tryptophan location, and base distribution in tobacco mosaic virus

Cheng¹

1968

Biochemistry

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“…mercury nitrate to give an S-methyl-mercury derivative [7] and with iodine to give a stable (!) sulfenyl iodide [8] (iodine also reacts with tyrosine Y 139, but not with Y2, Y70 and Y72 [9] Cooperative affinity labeling. If every capsomer of TMV carried a substituent group on its lysine K68 (which is located near the outer end of the capsomer [lo]), the substituents would be about 2.3 nm apart in the axial and 3.5 nm in the circumferencial direction.…”

Section: )mentioning

confidence: 97%

Section: )mentioning

confidence: 99%

Tobacco Mosaic Virus as a Carrier for Small Molecules I. The preparation and characterization of a TMV/α‐melanotropin conjugate

Kriwaczek¹,

Eberlé²,

Müller³

et al. 1978

Helvetica Chimica Acta

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SummaryThe use of tobacco mosaic virus (TMV) covalently loaded with hormones or other small molecules for various purposes including receptor detection and isolation is proposed. The basic principle is that of cooperative affinity interactions involving (large) numbers of artificially introduced sites (e.g. hormones) of the modified virus on the one hand and membrane-bound sites (e.g. receptors) of a cell or of a cellmembrane particle on the other. In order to test the feasibility of such TMV/hormone conjugates, TMV carrying about 500 molecules of a biologically active a -melanotropin analogue was synthesized, and characterized by its aspect under the electron microscope, by its infectivity, its melanophore-stimulating activity, and its reaction with antisera against a -melanotropin. The observed hormonal activity is in accordance with the idea of cooperative affinity interactions.The chemical nature of membrane-bound receptors for drugs and hormones is still an unsolved problem of molecular biology. This paper is the first of a series investigating the use of tobacco mosaic virus (TMV) covalently attached to hormones, drugs, and other comparatively small molecules for the study of receptors. First, some pertinent chemical properties of TMV and of polypeptide-hormone receptors are reviewed and the concept of cooperative affinity labelling is introduced. It is then demonstrated that some 500 molecules of an a-melanotropin (a-MSH) analogue can be covalently attached to the virus particle without destroying the essential chemical and biological properties characteristic of the virus and the hormone. I )This work was supported by the Swiss National Science Foundation. Abbreviations: TMV= tobacco mosaic virus; EM. = electron microscopy; symbols for amino acids and peptides according to the IUPAC-IUB rules [ 11.

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“…Of the four tyrosine residues, only 139 is readily available for iodination or acetylation [41,36]. Tyro-sine-2 is slowly available for reaction, while tyrosines-70 and 72 are unreactive.…”

Section: Surface Availability Of Residuesmentioning

confidence: 99%

A Prediction of the Structure of Tobacco-Mosaic-Virus Protein

Durham

Butler

1975

Eur J Biochem

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The location of amino acid residues within the tobacco mosaic virus protein subunit is discussed. Sequence data, X-ray crystallographic measurements, and the availability of specific residues for enzymic, immunological or chemical reaction are amongst the information used to trace roughly how the tobacco mosaic virus polypeptide chain winds in and out from the virus axis. Published rules for predicting secondary structure are then applied to obtain a diagram of the course of the polypeptide chain. This map should be useful for the interpretation of X-ray diffraction data and already permits an outline of the main features of the inner third of subunit to be suggested.Tobacco mosaic virus (TMV) protein presents a difficult problem for X-ray crystallographic structure determination. It can be crystallised as disks [1,2] but the asymmetric unit is very large (about 600000 daltons) and oriented gels of the virus itself are not sufficiently ordered to yield information to atomic resolution. Therefore, as an aid to the interpretation of current X-ray results, we attempt here to make deductions about the structure of the protein subunit from other available evidence. Such deductions impose limitations on the range of interactions between amino acid residues that may be proposed to explain other experimental data and, of course, the work also represents an exploration of the current state of the art of protein structure prediction.TMV protein is an unusually favourable subject for structure prediction because so much is already known about it. The information summarised here was obtained by many methods, the most important of which is X-ray crystallography, but also including electron microscopy, amino acid sequencing, titration studies and studies of the chemical, enzymic and immunological reactivity of various amino acid residues. The secondary structure of the polypeptide chain is then predicted, using the rules of Chou and Fasman [3,4]. Together these results enable us to propose a diagram of the approximate path of the polypeptide chain. Earlier attempts at partial TMV protein structure prediction have been made by Schiffer and Edmundson [5], and Leberman [7]. We gladly acknowledge that our thinking is based upon the labours of many people, not always explicitly mentioned here. In particular we acknowledge our debt to the crystallographic studies of Dr K. C. Holmes and his colleagues, started in Cambridge and continued, more recently, in Heidelberg. Low-Resolution Structural InformationThe TMV protein subunit contains 158 amino acid residues and has a molecular weight of 17493 [8,9]. Electron microscope and X-ray studies upon the virus (reviewed by Klug and Caspar [lo] and more recently by Barrett et al. [ll]) show that each subunit can be contained within a sector-shaped domain, like a slice of cake, within an angle of about 22". It extends radially from about 20 8, to about 90 8, from the virus helix axis, and is about 25 8, high. The RNA fits between the protein subunits in a groove at a radius of about 40 A,...

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Reactivity of the tyrosine residues of tobacco mosaic virus protein with iodine

Cited by 24 publications

References 12 publications

Optical rotatory dispersion, tryptophan location, and base distribution in tobacco mosaic virus

Optical rotatory dispersion, tryptophan location, and base distribution in tobacco mosaic virus

Tobacco Mosaic Virus as a Carrier for Small Molecules I. The preparation and characterization of a TMV/α‐melanotropin conjugate

A Prediction of the Structure of Tobacco-Mosaic-Virus Protein

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