Ribonucleic acid-protein cross-linking in Escherichia coli ribosomes: (4-azidophenyl)glyoxal, a novel heterobifunctional reagent

Politz, Samuel M.; Noller, Harry F.; McWhirter, Paul D.

doi:10.1021/bi00505a023

Cited by 23 publications

(11 citation statements)

References 41 publications

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“…In order to determine the amino acid sequence of M1 that binds to RNA, we cross-linked M1 to an oligoribonucleotide using APG, which binds covalently to guanine (Politz et al, 1981). The azido group in APG is then photolysed by UV light ( 300 nm) yielding an unstable nitrene which is potentially reactive with many groups in proteins and nucleic acids.…”

Section: Resultsmentioning

confidence: 99%

Influenza virus M1 protein binds to RNA through its nuclear localization signal.

Elster

Larsen

Gagnon

et al. 1997

Journal of General Virology

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The RNA-binding activity of influenza A virus M1 protein was studied by cross-linking the protein to viral RNA followed by sequence analysis of the oligoribonucleotide bound to the protein as well as sequence analysis of the M1 peptide bound to the RNA. M1 was found to bind to RNA without any RNA sequence specificity, as verified in a series of filterbinding experiments using a large variety of nucleic acids including DNA. The peptide sequence that bound to the RNA was the RKLKR nuclear

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Section: Resultsmentioning

confidence: 99%

Influenza virus M1 protein binds to RNA through its nuclear localization signal.

Elster

Larsen

Gagnon

et al. 1997

Journal of General Virology

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“…1C. This reagent, pazidophenyl glyoxal, was designed for protein-nucleic acid cross-linking and has been used specifically for the crosslinking of 16S rRNA to 30S ribosomal proteins of Escherichia coli (22). Such 1,2-dicarbonyl reagents as cyclohexanedione, glyoxal, and substituted glyoxals have been used in previous studies for the modification of arginine residues…”

Section: Resultsmentioning

confidence: 99%

“…in proteins (11,21,22). We considered it worthwhile to use p-azidophenyl glyoxal in our cross-linking studies, because major constituents of the nucleoprotein core, polypetides VII and ,u, are rich in arginine and poor in lysine residues ( Fig.…”

Section: Resultsmentioning

confidence: 99%

“…Protein-protein cross-linking with p-azidophenyl glyoxal was performed by incubation of the sample in 10 mM sodium borate (pH 8.3) containing 1% Triton X-100 and 5 mM cross-linker (dissolved in DMSO) in the dark for 30 min at room temperature, a method modified from that of Politz et al (22). Half of the sample was then irradiated for 5 min with light from a 200-W mercury arc lamp with a 5-mm-thick borosilicate glass plate to remove UV light of wavelength less than 320 nm.…”

Section: Methodsmentioning

confidence: 99%

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Interactions among the three adenovirus core proteins

Chatterjee¹,

Vayda²,

Flint³

1985

J Virol

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Interactions among the three adenovirus core polypeptides V, VII, and ,u were examined, using the reversible chemical cross-linker dithiobis(succinimidyl propionate) and two-dimensional polyacrylamide gel electrophoresis. Cross-linked species obtained from gradient-purified adenovirus type 2 cores were well represented among the cross-linked products of pentonless virions and crude core preparations. The more efficiently formed cross-linked core species were also identified with the arginine-specific cross-linker, p-azidophenyl glyoxal. In addition to dimers of polypeptides V and VII, efficient cross-linking of V to VII, V to ,I, and VII to V to ,u was detected in adenovirus cores. Notably absent were cross-linked species corresponding to higher multimers of polypeptide VII. A major core-capsid interaction appeared to be via the association of polypeptide V with a dimer of polypeptide VI.

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“…This cross-linking process is based on the initial specific derivatization of F-actin at the arginyl residues in positions 95 and 28 with p-azidophenylglyoxal which spans a cross-linking distance of approximately 0.7 nm (Ngo et al, 1981;Politz et al, 1981;Sgro et al, 1986). These arginine residues are within the actin subdomain-1 and form part of surface-exposed loop segments which were previously reported to participate in the attachment of actin to the S1 heavy chain (Bertrand et al, 1988;Mkjean et al, 1987;LabbC et al, 1990;Kabsch et al, 1990).…”

mentioning

confidence: 99%

Photochemical cross‐linking of the skeletal myosin head heavy chain to actin subdomain‐1 at Arg95 and Arg28

Bonafé

Chaussepied

Capony

et al. 1993

European Journal of Biochemistry

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F-actin specifically substituted with the photocross-linker, p-azidophenylglyoxal, at Arg95 and Arg28 was isolated and characterized. Upon complexation with myosin subfragment-1 (Sl) and photolysis at 365 nm, it was readily cross-linked to the S1 heavy chain with a yield of about 13-25 %, generating four major actin-heavy-chain adducts with molecular masses in the range 165-240 kDa. The elevated Mg2'-ATPase of the covalent complexes displayed a turnover rate of 33 ? 8 s-I which is similar to the values reported earlier for other acto-S1 conjugates. The crosslinking between various proteolytic S1 and actin derivatives, combined with the fluorescent and immunochemical detection of the photocross-linked products, indicated that the arylnitrene group on Arg95 was inserted predominantly in the central 50-kDa region, whereas that attached to Arg28 mediated the selective cross-linking of the COOH-terminal 22-21-kDa fragments of the heavy chain, most probably by reacting at or near the connector segment between the 50-kDa and 20-kDa fragments. The rapid photoactivation and cross-linking to S1 of the substituted F-actin, which can be accomplished on a millisecond time scale, may serve to probe the structural dynamics of the interaction of the S1 heavy chain with subdomain-1 of actin during the ATPase cycle.During muscle contraction, the cyclic interactions between F-actin and the myosin heads or myosin subfragment-1 (Sl) are essential for the conversion of ATP hydrolysis into contractile force by the actomyosin-ATP complex. The nature of the nucleotide intermediates bound to the ATPase site is thought to determine the molecular movements and attitudes of the myosin heads over the actin filament (Botts et al., 1984;Huxley and Kress, 1985;Vibert and Cohen, 1988). The changes in the structure, localization and affinity of the binding sites at the actin-S1 interface would, therefore, play a major role in the transients of the displacement of S1 along F-actin.At present, it can be postulated that the generation of any acto-S 1 complex involves the specific association between the subdomain-1 of actin, the outermost domain of the actin protomere in the filament, containing all the known putative S1 interactive sites (Holmes et al., 1990;Milligan et al., 1990), and polypeptide stretches of the 20-kDa and 50-kDa fragments of the S1 heavy chain, the two potent actin-binding regions so far identified in the native protein (Mornet et Correspondence to P. Chaussepied or R.

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Ribonucleic acid-protein cross-linking in Escherichia coli ribosomes: (4-azidophenyl)glyoxal, a novel heterobifunctional reagent

Cited by 23 publications

References 41 publications

Influenza virus M1 protein binds to RNA through its nuclear localization signal.

Influenza virus M1 protein binds to RNA through its nuclear localization signal.

Interactions among the three adenovirus core proteins

Photochemical cross‐linking of the skeletal myosin head heavy chain to actin subdomain‐1 at Arg95 and Arg28

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