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Academic literature on the topic 'Myristylation'
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Journal articles on the topic "Myristylation"
1
Garber, E. A., F. R. Cross, and H. Hanafusa. "Processing of p60v-src to its myristylated membrane-bound form." Molecular and Cellular Biology 5, no. 10 (1985): 2781–88. http://dx.doi.org/10.1128/mcb.5.10.2781.
Full textAbstract:
p60src of wild-type Rous sarcoma virus is myristylated at its N-terminal glycine residue. We have shown previously that this myristylation is necessary for p60src membrane association and for cell transformation by using src mutants with alterations within the N-terminal 30 kilodaltons of p60src. In this study we analyzed the process of p60src myristylation in wild type- and mutant-infected cells. All myristylated src proteins examined lack the initiator methionine, but two mutant src proteins lacking the initiator methionine are not myristylated, indicating that removal of the initiator methionine and myristylation are not obligatorily coupled. Analysis of the kinetics of myristylation and the association of p60src with cellular proteins p50 and p90 indicated that myristylation occurs before p60src becomes membrane associated and that transient association with p50 and p90 occurs regardless of myristylation. Myristylation is required for stable association of p60src with the plasma membrane but is not sufficient for membrane association. A mutant with an src deletion of amino acids 169 through 264 has an src protein that is myristylated but not membrane bound, remaining stably associated with p50 and p90. This mutant is transformation defective. Several N-terminal deletion mutants possessing tyrosine kinase activity have myristylated and membrane-bound src proteins but are not fully active in cell transformation, suggesting that additional N-terminal functional domains exist.
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Garber, E. A., F. R. Cross, and H. Hanafusa. "Processing of p60v-src to its myristylated membrane-bound form." Molecular and Cellular Biology 5, no. 10 (1985): 2781–88. http://dx.doi.org/10.1128/mcb.5.10.2781-2788.1985.
Full textAbstract:
p60src of wild-type Rous sarcoma virus is myristylated at its N-terminal glycine residue. We have shown previously that this myristylation is necessary for p60src membrane association and for cell transformation by using src mutants with alterations within the N-terminal 30 kilodaltons of p60src. In this study we analyzed the process of p60src myristylation in wild type- and mutant-infected cells. All myristylated src proteins examined lack the initiator methionine, but two mutant src proteins lacking the initiator methionine are not myristylated, indicating that removal of the initiator methionine and myristylation are not obligatorily coupled. Analysis of the kinetics of myristylation and the association of p60src with cellular proteins p50 and p90 indicated that myristylation occurs before p60src becomes membrane associated and that transient association with p50 and p90 occurs regardless of myristylation. Myristylation is required for stable association of p60src with the plasma membrane but is not sufficient for membrane association. A mutant with an src deletion of amino acids 169 through 264 has an src protein that is myristylated but not membrane bound, remaining stably associated with p50 and p90. This mutant is transformation defective. Several N-terminal deletion mutants possessing tyrosine kinase activity have myristylated and membrane-bound src proteins but are not fully active in cell transformation, suggesting that additional N-terminal functional domains exist.
3
Clark, B., and U. Desselberger. "Myristylation of Rotavirus Proteins." Journal of General Virology 69, no. 10 (1988): 2681–86. http://dx.doi.org/10.1099/0022-1317-69-10-2681.
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Kaplan, J. M., G. Mardon, J. M. Bishop, and H. E. Varmus. "The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant." Molecular and Cellular Biology 8, no. 6 (1988): 2435–41. http://dx.doi.org/10.1128/mcb.8.6.2435.
Full textAbstract:
The transforming protein of Rous sarcoma virus, pp60v-src, is covalently coupled to myristic acid by an amide linkage to glycine 2. Myristylation promotes the association of pp60v-src with cellular membranes, and this subcellular location is essential for transforming activity. The findings presented here, in conjunction with the previous reports of others, imply that the seventh amino acid encoded by v-src might be important in the myristylation reaction. Replacement of lysine 7 by asparagine greatly reduced the myristylation, membrane association, and transforming activity of pp60v-src. In contrast, substitution of arginine at residue 7 had no effect on any of these properties of pp60v-src. Addition of amino acids 1 to 7 encoded by v-src was sufficient to cause myristylation of a src-pyruvate kinase fusion protein. We conclude that the recognition sequence for myristylation of pp60v-src comprises amino acids 1 to 7 and that lysine 7 is a critical component of this sequence.
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Kaplan, J. M., G. Mardon, J. M. Bishop, and H. E. Varmus. "The first seven amino acids encoded by the v-src oncogene act as a myristylation signal: lysine 7 is a critical determinant." Molecular and Cellular Biology 8, no. 6 (1988): 2435–41. http://dx.doi.org/10.1128/mcb.8.6.2435-2441.1988.
Full textAbstract:
The transforming protein of Rous sarcoma virus, pp60v-src, is covalently coupled to myristic acid by an amide linkage to glycine 2. Myristylation promotes the association of pp60v-src with cellular membranes, and this subcellular location is essential for transforming activity. The findings presented here, in conjunction with the previous reports of others, imply that the seventh amino acid encoded by v-src might be important in the myristylation reaction. Replacement of lysine 7 by asparagine greatly reduced the myristylation, membrane association, and transforming activity of pp60v-src. In contrast, substitution of arginine at residue 7 had no effect on any of these properties of pp60v-src. Addition of amino acids 1 to 7 encoded by v-src was sufficient to cause myristylation of a src-pyruvate kinase fusion protein. We conclude that the recognition sequence for myristylation of pp60v-src comprises amino acids 1 to 7 and that lysine 7 is a critical component of this sequence.
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Kamata, N., and J. T. Holt. "Inhibitory effect of myristylation on transrepression by FBR (Gag-Fos) protein." Molecular and Cellular Biology 12, no. 2 (1992): 876–82. http://dx.doi.org/10.1128/mcb.12.2.876.
Full textAbstract:
The myristylated v-fos product, FBR murine sarcoma virus (Gag-Fos) protein, exhibits a lower level of transrepression of the serum response element (SRE) than does c-fos protein (Fos). Mutation of the N-terminal myristylation site in FBR protein restored SRE transrepression. Replacement of N-terminal viral Gag sequences with the Fos N terminus also restored this activity, providing additional evidence that myristylation inhibits transrepression by FBR protein. However, the myristylated Gag domain did not inhibit SRE transrepression when fused to Fos, indicating that myristylation of a fos protein is not by itself sufficient to prevent SRE transrepression and that C-terminal mutation is necessary to inhibit transrepression by N myristylation. Comparison of transfection results with Fos C-terminal deletion mutants and the Fos/FBR chimeric mutant revealed that the FBR C terminus retained the potential for transrepression despite deletion of the normal Fos C terminus, whereas similar Fos deletion mutants did not. These results indicate that both N- and C-terminal mutations are required to inhibit transrepression by FBR protein and that multiple structural mutations accompanied by posttranslational protein modification alter gene regulation by FBR protein.
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Kamata, N., and J. T. Holt. "Inhibitory effect of myristylation on transrepression by FBR (Gag-Fos) protein." Molecular and Cellular Biology 12, no. 2 (1992): 876–82. http://dx.doi.org/10.1128/mcb.12.2.876-882.1992.
Full textAbstract:
The myristylated v-fos product, FBR murine sarcoma virus (Gag-Fos) protein, exhibits a lower level of transrepression of the serum response element (SRE) than does c-fos protein (Fos). Mutation of the N-terminal myristylation site in FBR protein restored SRE transrepression. Replacement of N-terminal viral Gag sequences with the Fos N terminus also restored this activity, providing additional evidence that myristylation inhibits transrepression by FBR protein. However, the myristylated Gag domain did not inhibit SRE transrepression when fused to Fos, indicating that myristylation of a fos protein is not by itself sufficient to prevent SRE transrepression and that C-terminal mutation is necessary to inhibit transrepression by N myristylation. Comparison of transfection results with Fos C-terminal deletion mutants and the Fos/FBR chimeric mutant revealed that the FBR C terminus retained the potential for transrepression despite deletion of the normal Fos C terminus, whereas similar Fos deletion mutants did not. These results indicate that both N- and C-terminal mutations are required to inhibit transrepression by FBR protein and that multiple structural mutations accompanied by posttranslational protein modification alter gene regulation by FBR protein.
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Kamata, N., R. M. Jotte, and J. T. Holt. "Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein." Molecular and Cellular Biology 11, no. 2 (1991): 765–72. http://dx.doi.org/10.1128/mcb.11.2.765.
Full textAbstract:
FBR murine sarcoma virus (gag-fos) protein, a virally transduced Fos protein, exhibits decreased gene transactivation in comparison with the cellular Fos protein. Biochemical analysis suggests that myristylation of the virally encoded N-terminal gag region results in decreased DNA binding and transcriptional activation without affecting heterodimerization with Jun protein. These findings demonstrate that protein myristylation can modulate gene regulation by a DNA-binding protein.
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Kamata, N., R. M. Jotte, and J. T. Holt. "Myristylation alters DNA-binding activity and transactivation of FBR (gag-fos) protein." Molecular and Cellular Biology 11, no. 2 (1991): 765–72. http://dx.doi.org/10.1128/mcb.11.2.765-772.1991.
Full textAbstract:
FBR murine sarcoma virus (gag-fos) protein, a virally transduced Fos protein, exhibits decreased gene transactivation in comparison with the cellular Fos protein. Biochemical analysis suggests that myristylation of the virally encoded N-terminal gag region results in decreased DNA binding and transcriptional activation without affecting heterodimerization with Jun protein. These findings demonstrate that protein myristylation can modulate gene regulation by a DNA-binding protein.
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Loh, Ying-Tsu, Jianmin Zhou, and Gregory B. Martin. "The Myristylation Motif of Pto Is Not Required for Disease Resistance." Molecular Plant-Microbe Interactions® 11, no. 6 (1998): 572–76. http://dx.doi.org/10.1094/mpmi.1998.11.6.572.
Full textAbstract:
The tomato Pto kinase confers resistance to bacterial speck disease caused by strains of Pseudomonas syringae pv. tomato that express the avirulence gene avrPto. Pto contains a putative myristylation site at its amino terminus that was hypothesized to play a role in localizing Pto in the plant cell. Site-directed mutagenesis was used to change the invariant glycine residue in the myristylation motif to an alanine. Transgenes encoding the mutant Pto(G2A) and wild-type Pto were placed behind the cauliflower mosaic virus 35S promoter and transformed into tomato plants that are susceptible to bacterial speck disease. Both the mutant and wild-type forms of Pto conferred resistance to a strain of P. syringae pv. tomato expressing avrPto. These results indicate that the myristylation motif of Pto is not required for bacterial speck disease resistance.
Dissertations / Theses on the topic "Myristylation"
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Marc, Daniel. "La myristylation de la proteine de capside vp4 du poliovirus; son role dans le cycle viral." Paris 7, 1991. http://www.theses.fr/1991PA077059.
Full textAbstract:
La proteine de capside vp4 du poliovirus, ainsi que des precurseurs vp0 et p1, est myristlee: sa glycine n-terminale est liee de maniere covalente a un acide gras tetra-decanoique. Cette modification co-traductionnelle est determinee par la sequence n-terminale de la proteine (gly#1ala#2gln#3val#4ser#5ser#6). Par mutagenese dirigee a l'aide d'oligonucleotides, nous avons modifie dans le cadn viral la sequence codant pour le signal de myristylation de la proteine. Des transcrits genomiques portant les differentes mutations ont ete synthetises in vitro, et leurs proprietes analysees in vitro par traduction en systeme acellulaire, et in vivo apres transfection de cellules de primates. La transfection du transcrit portant la mutation ser#5thr conduit a une production de virus possedant une proteine normalement myristylee. Toutes les autres mutations qui empechent totalement (gly#1arg et gly#1ala) ou partiellement (ser#5pro et ala#2pro) la myristylation de la proteine vp0 in vivo, abolissent l'infectivite des transcrits. Ces dernieres mutations n'empechent pas la replication des transcrits in vivo, mais affectent la maturation proteolytique du precurseur p1 in vitro. En outre, dans le cas des mutations de la glycine no 1, l'assemblage viral n'a pas lieu, le defaut se situant au niveau de l'assemblage des pentameres 14s. Dans le cas des deux autres mutations (ser#5pro et ala#2pro), des particules virales matures s'assemblent en quantite reduite, mais ces virons ne sont pas infectieux et semblent defectueux dans les etapes precoces de l'infection. La myristylation de la proteine vp4 et de ses precurseurs est donc indispensable au cycle viral. Elle joue role important au niveau de l'assemblage viral, mais semble egalement impliquee dans les etapes precoces de la decapsidation
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Abou, Jaoude Georges. "Etude des protéines d'enveloppe du virus de l'hépatite B à l'étape d'entrée virale : utilisation du virus de l'hépatite Delta comme modèle expérimental." Paris 6, 2006. http://www.theses.fr/2006PA066331.
Full textAbstract:
Le virus de l’hépatite B (HBV) est un virus enveloppé à ADN. Sa nucléocapside est incluse dans une enveloppe composée de lipides et des protéines d’enveloppe virales dénommées grande (L), moyenne (M), et petite (S). Une caractéristique unique du cycle de réplication de l’HBV concerne le mécanisme d’assemblage des virions. Ces derniers sont produits en quantités mineures par rapport à l’abondante production de particules sous-virales (PSV) dépourvues de nucléocapside, que l’on retrouve en majorité dans un sérum infectieux. Les PSV sont constituées de lipides d’origine cellulaire et des protéines d’enveloppe HBV. Ces dernières assurent la dynamique d’assemblage des particules lipoprotéiques et recrutent la nucléocapside pour l’exporter sous forme de virions. Elles ont aussi la charge d’adresser les virions spécifiquement à la surface de la cellule cible, l’hépatocyte humain. Par ailleurs, les protéines d’enveloppe HBV peuvent également véhiculer la ribonucléoprotéine du virus de l’hépatite delta (HDV), un virus satellite occasionnel d’HBV dépourvu de système de propagation. Mon travail de thèse a consisté à étudier la fonction des protéines d’enveloppe HBV à l’entrée virale en utilisant le modèle HDV, et les cellules sensibles HepaRG. Il a permis de mettre en place un système sensible et fiable pour l’étude des fonctions des protéines d’enveloppe HBV à l’entrée virale. L’utilisation de ce système a permis de démontrer un rôle indispensable à l’entrée virale HDV du groupement myristate lié à la protéine L en son extrémité N-terminale. En outre, il a permis d’identifier, sur les protéines d’enveloppe, un nouveau déterminant d’infectiosité situé dans la boucle antigénique (BAG). Ce domaine constitue la cible principale des anticorps neutralisants, et il porte 8 résidus cystéine qui semblent jouer un rôle majeur à l’infection. La BAG porte donc un site actif à l’entrée virale qui pourrait faire l’objet d’un ciblage spécifique par de nouveaux antiviraux.
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Franco, Michel. "La petite proteine g arf (adp-ribosylation factor) : interaction avec les phospholipides, role de la myristylation. interaction avec la sous-unite beta-gamma de proteines g heterotrimeriques." Nice, 1995. http://www.theses.fr/1995NICE4867.
Full textAbstract:
Arf (adp-ribosylation factor) est une proteine g monomerique, de 21 kda, identifiee a l'origine comme etant le cofacteur de la toxine du cholera dans la reaction d'adp-ribosylation. Mais son role physiologique se situe dans le trafic des vesicules membranaires. Au niveau de l'appareil de golgi, arf est impliquee dans la formation et la fusion des vesicules. Par ses analogies de sequence en acides amines et la nature de sa modification lipidique, arf s'apparente plus a une sous-unite (g) de proteines g heterotrimeriques qu'a une petite proteine g membre de la super famille ras. Nous avons mis en evidence une autre caracteristique commune entre arf et g: la capacite de former un complexe avec le dimere b(gb). Arf est capable, dans sa conformation inactive d'interagir avec la sous-unite b de transducine (proteine g du systeme visuel). Cette interaction, independante de la presence de la modification lipidique de l'arf, est vraisemblablement permise par la conservation sur arf d'un domaine de g. La presence de ce site sur arf permettrait une connexion entre les voies d'action de ces deux types de proteines g. Arf est myristylee du cote n-terminal. Nous avons etudie l'effet de cette modification lipidique sur l'interaction de la proteine avec les phospholipides de la membrane ainsi que sur l'echange nucleotidique intrinseque ou catalyse par un facteur proteique. L'activation de l'arf stabilise la proteine sur la membrane phospholipidique. Nous demontrons que cette association est independante de la myristylation. De meme, nous montrons que l'activation de l'arf provoque la formation d'un complexe membranaire avec la toxine du cholera, independamment de la myristylation. Dans la forme inactive en revanche, nous observons que la myristylation est responsable d'une liaison partielle de l'arf a la membrane. La presence du myristate sur la proteine modifie la structure du site nucleotidique. Elle favorise la dissociation du gdp et permet, en presence de phospholipides, une activation spontanee. Nous demontrons que la myristylation est essentielle pour l'activation de l'arf par un facteur d'echange dont nous avons mis en evidence l'existence dans la retine
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Martin, Karen H. "Fatty acylation of Vaccinia virus proteins : dual myristylation and palmitylation of the A-type inclusion protein." Thesis, 1997. http://hdl.handle.net/1957/33994.
Full textAbstract:
The attachment of myristic acid to the N-terminal glycine residue of many
eukaryotic and viral proteins is often essential for the acquisition of the protein's
biological activity. Vaccinia virus (VV), the prototype member of the Poxviridae,
expresses several myristylated proteins during the course of infection. Only one of
these proteins, L1R, has been identified and characterized.
Experiments were performed to identify and analyze four additional VV
myristylproteins. These proteins were identified as the A-type inclusion protein (92
kDa), G9R (39 kDa), A16L (36 kDa), and E7R (17 kDa). The latter three proteins
were shown to be myristylated on an N-terminal glycine residue. Additional studies
demonstrated that both A16L and E7R are soluble proteins, unlike L1R, which is a
constituent of the viral envelope. Furthermore, A16L could not be detected in either purified extracellular enveloped virus (EEV) or in intracellular mature virus (IMV).
These are the two predominant forms of infectious virions produced during a VV
infection. E7R was detected in EEV and, to a lesser extent, in IMV.
Unlike the other proteins, the amino terminal sequence of the A-type inclusion
protein did not fit the consensus sequence for N-myristylation (M-G-X-X-X-S/T/A/C/N), suggesting that it was internally myristylated. A combination of studies
revealed that the protein is both myristylated and palmitylated. Addition of each acyl
group could be separated temporally: myristylation occured co-translationally, while
palmitylation occurred post-translationally. Genetic analyses of lysine doublets and
arginine/lysine doublets within the A-type inclusion protein indicated that these sites
are not utilized for myristylation. This is in contrast to the precursors of TNFoc and Ilia
which are internally-myristylated on a lysine doublet.
It is not clear why this protein would be both myristylated and palmitylated.
Only class four palmitylproteins, such as the Src family of proteins, have been shown
to be both myristylated and palmitylated. The A-type inclusion protein expressed by
cowpox virus forms a large symmetrical matix in the cytoplasm of infected cells and
generally contains mature virions. It is possible, therefore, that the function of
acylation may be to stabilize the protein matrix or to assist in occlusion of enveloped
virus particles.<br>Graduation date: 1998
Books on the topic "Myristylation"
1
Martin, Karen H. Fatty acylation of Vaccinia virus proteins: Dual myristylation and palmitylation of the A-type inclusion protein. 1997.
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