Association of cyclic GMP with gene expression of polytene chromosomes of Drosophila melanogaster.

Spruill, W A; Hurwitz, David R.; Lucchesi, John C.; Steiner, Alton L.

doi:10.1073/pnas.75.3.1480

Cited by 33 publications

(8 citation statements)

References 45 publications

(37 reference statements)

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“…These observations suggest that perhaps cGMP and the cGMPbinding protein are involved in regulating gene expression. Bound cGMP has been found associated with puffed areas of polytene chromosomes in Drosophila melanogaster (38). Also, cGMP has been reported to affect DNA-dependent RNA polymerase activity in lymphocytes (39).…”

Section: Discussionmentioning

confidence: 99%

Relationship of the cGMP-binding activity to the cGMP-specific phosphodiesterase in Dictyostelium discoideum

Parissenti¹,

Coukell²

1986

Biochem. Cell Biol.

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Parissenti, A. M. & Coukell, M. B. (1986) Relationship of the cGMP-binding activity to the cGMP-specific phosphodiesterase in Dictyostelium discoideum. Biochem. Cell Biol. 64, 528-534 Optimal conditions for assaying and stabilizing the soluble cGMP-binding activity in Dictyostelium discoideum were established. Using these procedures, we investigated the relationship between the cGMP-binding activity and the cGMP-specific phosphodiesterase in this organism. In wild-type strains, the binding and phosphodiesterase activities were found to be regulated differently during development. Also, stmF mutants, which possess very low levels of cGMP-specific phosphodiesterase activity, exhibited normal levels of cGMP-binding activity. Fractionation studies revealed that the binding and phosphodiesterase activities could be resolved by DEAE-cellulose chromatography. Finally, the effect of pH on cGMP binding was different from that reported for cGMP-mediated activation of the phosphodiesterase. Taken together, these results indicate that the cGMP-binding protein and the cGMP-specific phosphodiesterase are probably unrelated. In addition, the cGMP-binding activity is not associated with cGMP-stimulated kinase activity and it does not elute from DEAE-cellulose like the highly conserved cGMP-dependent protein kinases found in other systems. Parissenti, A. M. & Coukell, M. B. (1986) Relationship of the cGMP-binding activity to the cGMP-specific phosphodiesterase in Dictyostelium discoideum. Biochem. Cell Biol. 64, 528-534 Nous avons ktabli les conditions optimales pour I'essai et la stabilisation de I'activitk de liaison du cGMP soluble chez Dictyostelium discoideum. Ces techniques nous ont permis de rechercher la relation entre l'activitk de liaison du cGMP et la phosphodiestkrase spkcifique du cGMP chez cet organisme. Dans les souches de type sauvage, l'activite de liaison et I'activitk phosphodiestkrasique sont contr6ltes de faqon diffkrente durant le developpement.De plus, les mutants stmF, chez qui l'activitk de la phosphodiestkrase spkcifique du cGMP est trbs basse, prksentent des taux normaux d'activit6 de liaison du cGMP. Les etudes de fractionnement r6vtlent que I'activite de liaison peut &tre skpar6e de l'activitk phosphodiest6rasique par chromatographic sur DEAE-cellulose. Finalement, l'effet du pH sur la liaison du cGMP differe de l'effet rapport6 pour I'activation par le cGMP de la phosphodiesttrase. Globalement, ces rksultats suggkrent l'absence probable de relation entre la protkine de liaison du cGMP et la phosphodiesttrase spkcifique du cGMP. De plus, I'activitk de liaison du cGMP n'est pas associke a l'activitk kinasique stirnulee par le cGMP et elle n'klue pas de la DEAE-cellulose comme les protkine kinases dtpendantes du cGMP et hautement conservBes, retrouvkes dans d'autres systbmes.[Traduit par la revue]

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Section: Discussionmentioning

confidence: 99%

Relationship of the cGMP-binding activity to the cGMP-specific phosphodiesterase in Dictyostelium discoideum

Parissenti¹,

Coukell²

1986

Biochem. Cell Biol.

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“…The significance of an early observation of Spruill et al (1978) that cyclic-GMP is present at many active chromosome sites in control cells but preferentially accumulates at the 93D puff following heat shock also remains unknown. In the context of the accumulation hnRNPs, etc., on the 93D puff in heat-shocked cells, it will be interesting to examine if cyclic-GMP is involved in some modifications of the hnRNPs while they are sequestered at the 93D puff.…”

Section: Association Of Different Hnrnps and Other Proteins With Hsrωmentioning

confidence: 95%

Forty years of the 93D puff of Drosophila melanogaster

Lakhotia

2011

J Biosci

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The 93D puff of Drosophila melanogaster became attractive in 1970 because of its singular inducibility by benzamide and has since then remained a major point of focus in my laboratory. Studies on this locus in my and several other laboratories during the past four decades have revealed that (i) this locus is developmentally active, (ii) it is a member of the heat shock gene family but selectively inducible by amides, (iii) the 93D or heat shock RNA omega (hsr row) gene produces multiple nuclear and cytoplasmic large non-coding RNAs (hsr row-n, hsr row-pre-c and hsr row-c), (iv) a variety of RNA-processing proteins, especially the hnRNPs, associate with its > 10 kb nuclear (hsr row-n) transcript to form the nucleoplasmic omega speckles, (v) its genomic architecture and hnRNP-binding properties with the nuclear transcript are conserved in different species although the primary base sequence has diverged rapidly, (vi) heat shock causes the omega speckles to disappear and all the omega speckle associated proteins and the hsr row-n transcript to accumulate at the 93D locus, (vii) the hsr row-n transcript directly or indirectly affects the localization/ stability/activity of a variety of proteins including hnRNPs, Sxl, Hsp83, CBP, DIAP1, JNK-signalling members, proteasome constituents, lamin C, ISWI, HP1 and poly(ADP)-ribose polymerase and (viii) a balanced level of its transcripts is essential for the orderly relocation of various proteins, including hnRNPs, RNA pol II and HP1, to developmentally active chromosome regions during recovery from heat stress. In view of such multitudes of interactions, it appears that large non-coding RNAs like those produced by the hsr row gene may function as hubs to coordinate multiple cellular networks and thus play important roles in maintenance of cellular homeostasis.

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“…For heat-shock experiments the salivary glands were incubated at 37°C for 30 min in Drosophila PBS. After 30-min incubation, the label was removed with a syringe and 100 pl of formaldehyde fixative solution (22) was added. After a 20-min incubation, 20 pl of cold 20% TCA was added and the glands were then transferred to 3 ml of the same solution and incubated for 10 min at 0°C.…”

Section: Heat Shockmentioning

confidence: 99%

“…It is highly unlikely that the extensive labeling of chromosomes by [3 H]DFP is caused by any relocation of cytoplasmic DFP-binding protein to the chromosome during the prepara- RESULTS AND DISCUSSION tion of the chromosome squash because the whole salivary glands were fixed with formaldehyde before squashing. Using this procedure it was shown that cyclic GMP, but not cyclic AMP, is associated with the heat-shock specific puffs (22). Both of these compounds are diffusible nucleotides, and it is highly unlikely that cyclic GMP, but not cyclic AMP, would associate with specific loci of chromosomes if they are relocated during the preparation of polytene chromosomes .…”

Section: Embryo Chromatinmentioning

confidence: 99%

Association of a protease with polytene chromosomes of Drosophila melanogaster.

Cavagnaro¹,

Pierce²,

Lucchesi³

et al. 1980

The Journal of Cell Biology

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Incubation of Drosophila salivary glands with radioactive diisopropyl fluorophosphate results in the uniform labeling of polytene chromosomes. Extensive labeling is seen only when chromosome squashes are prepared by a formaldehyde fixation procedure and not by standard acetic acid techniques . The labeling is inhibited in the presence of tosylphenylalanine chloromethyl ketone and phenylmethane sulfonylfluoride but not by tosyllysine chloromethyl ketone, suggesting that a chymotrypsin-like serine protease is associated with the chromosomes. Protease inhibitors show no apparent effect on heat-shock specific puffing.Chromatin isolated from various rat and mouse tissues contains a highly basic 25,000-dalton serine protease (3), which appears to be directly bound to the DNA (J. Cavagnaro and C.-B . Chae, manuscript submitted for publication) . The protease selectively cleaves H 1 histone in condensed but not in relaxed chromatin (11,12) and oligonucleosomes in vitro (Y.-J . Kim and C.-B . Chae, unpublished results), suggesting the possibility of involvement of the enzyme in the local decondensation of super-coiled chromatin fiber by controlled cleavage of H 1 histone in vivo . The polytene chromosomes of Drosophila melanogaster larval salivary glands are an excellent system with which to study this possibility because specific genes at certain loci can be activated by heat and this gene activation accompanies readily recognizable puffing at the heat-shock specific loci (18). Therefore, we have attempted to establish that a protease is associated with polytene chromosomes by labeling chromosomes with a radioactive active site-directed protease inhibitor, diisopropyl fluorophosphate (DFP) and have studied the possible effect of protease inhibitors on heat-shock specific puffing.We find that although a chymotrypsin-like protease appears to be uniformly distributed along the polytene chromsomes, protease inhibitors do not appear to affect the specific puffing elicited by heat shock . After incubation the glands were transferred to formaldehyde fixative for 1-2 min and then squashed in formaldehyde-acetic acid (22) onto a subbed slide . The slide was then dipped into liquid nitrogen. Immediately after dipping, the covershp was removed with a razor blade and the slide was placed in cold PBS for 30-120 min with three changes of buffer . After the last rinse in PBS, the slides were prepared for autoradiography. Autoradiography and Giemsa staining were performed as previously described (15). MATERIALS AND METHODS Labeling of Salivary Heat ShockFor heat-shock experiments the salivary glands were incubated at 37°C for 30 min in Drosophila PBS. SDS Gel Electrophoresis of ( 3 HJDFP-labeledProteins 20 salivary glands were incubated in 100 pl of Drosophila phosphate-buffered solution with or without inhibitor and incubated for 30 min át room temperature. The solution was removed with a tuberculin syringe and 100 pl of [a H]DFP in PBS (final concentration 6.15 x 10 -s M [ 3H]DFP) was applied to cover the glands . After 30-m...

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Association of cyclic GMP with gene expression of polytene chromosomes of Drosophila melanogaster.

Cited by 33 publications

References 45 publications

Relationship of the cGMP-binding activity to the cGMP-specific phosphodiesterase in Dictyostelium discoideum

Relationship of the cGMP-binding activity to the cGMP-specific phosphodiesterase in Dictyostelium discoideum

Forty years of the 93D puff of Drosophila melanogaster

Association of a protease with polytene chromosomes of Drosophila melanogaster.

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