Temporal expression patterns of diapause-associated genes in flesh fly pupae from the onset of diapause through post-diapause quiescence

Hayward, Scott A. L.; Pavlides, Savvas C.; Tammariello, Steven P.; Rinehart, Joseph P.; Denlinger, David L.

doi:10.1016/j.jinsphys.2004.11.009

Cited by 124 publications

(77 citation statements)

References 34 publications

Supporting

Mentioning

Contrasting

Unclassified

Order By: Relevance

“…In most cases, expression of Hsps is incompatible with progression of development. Overexpression of Hsp70 results in a retardation of cell cycle progression (16) and a slowing of development in Drosophila melanogaster (46), and we have demonstrated that the onset of adult development is delayed when Hsps are being produced (47). We thus suspect that the presence of Hsps during diapause not only contributes to the enhancement of cold tolerance but also provides a secondary mechanism for assuring that development remains arrested.…”

Section: Resultsmentioning

confidence: 98%

Up-regulation of heat shock proteins is essential for cold survival during insect diapause

Rinehart

Yocum

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

476

409

View full text Add to dashboard Cite

Diapause, the dormancy common to overwintering insects, evokes a unique pattern of gene expression. In the flesh fly, most, but not all, of the fly's heat shock proteins (Hsps) are up-regulated. The diapause up-regulated Hsps include two members of the Hsp70 family, one member of the Hsp60 family (TCP-1), at least four members of the small Hsp family, and a small Hsp pseudogene. Expression of an Hsp70 cognate, Hsc70, is uninfluenced by diapause, and Hsp90 is actually down-regulated during diapause, thus diapause differs from common stress responses that elicit synchronous up-regulation of all Hsps. Up-regulation of the Hsps begins at the onset of diapause, persists throughout the overwintering period, and ceases within hours after the fly receives the signal to reinitiate development. The up-regulation of Hsps appears to be common to diapause in species representing diverse insect orders including Diptera, Lepidoptera, Coleoptera, and Hymenoptera as well as in diapauses that occur in different developmental stages (embryo, larva, pupa, adult). Suppressing expression of Hsp23 and Hsp70 in flies by using RNAi did not alter the decision to enter diapause or the duration of diapause, but it had a profound effect on the pupa's ability to survive low temperatures. We thus propose that up-regulation of Hsps during diapause is a major factor contributing to cold-hardiness of overwintering insects.cold tolerance ͉ overwintering ͉ stress proteins ͉ RNAi

show abstract

Section: Resultsmentioning

confidence: 98%

Up-regulation of heat shock proteins is essential for cold survival during insect diapause

Rinehart

Yocum

et al. 2007

Proc. Natl. Acad. Sci. U.S.A.

476

409

View full text Add to dashboard Cite

show abstract

“…Proteins that are less abundant in diapausing larvae could potentially be just as important as proteins that are unique to diapause or are more abundant during diapause. At the transcript level, for example, down-regulation of the cell cycle regulator, Proliferating Cell Nuclear Antigent, appears to be a key feature in shutting down the cell cycle during diapause in the flesh fly (Hayward et al, 2005).…”

Section: Discussionmentioning

confidence: 99%

Proteomic analysis of pre-diapause, diapause and post-diapause larvae of the wheat blossom midge, Sitodiplosis mosellana (Diptera: Cecidomyiidae)

Cheng¹,

Li²,

Yu³

et al. 2009

Eur. J. Entomol.

View full text Add to dashboard Cite

Abstract. To determine the relationship between protein expression and insect diapause, a proteomic approach was used to investigate the proteins extracted from larvae of the wheat blossom midge Sitodiplosis mosellana Gehin at different developmental stages, including pre-diapause, over-summering diapause, over-wintering diapause and post-diapause. Using 2-DE gels stained with coomassie brilliant blue, about 300 protein spots were detected in the extracts of pre-diapause larvae and 275 for those in each of the other stages. There were 91, 92 and 95 protein spots that showed more than a 2-fold change in abundance in the over-summering diapause, over-wintering diapause and post-diapause stages compared with pre-diapause. Eight protein spots, which showed the greatest difference in the larvae at different stages of diapause, were analyzed using Matrix-assisted laser desorption ionization time of flight mass spectrometry (MALDI-TOF-MS). Seven of them were successfully identified from their peptide mass fingerprints using the NCBInr database. They were proopiomelanocortin, NADH dehydrogenase subunit 1 and F10F2.5, which were up-regulated or unique to pre-diapause larvae, IKK interacting protein isoform 2 up-regulated in diapause and post-diapause larvae, GA10647-PA unique in over-wintering diapause larvae, purple CG16784-PB isoform B and B0228.6 up-regulated in over-summering and overwintering diapause larvae. The potential functions of these proteins during wheat blossom midge diapause are discussed.

show abstract

“…66 Among insects, mRNA transcript levels of hsp23 and hsp70 were upregulated throughout pupal diapause in the flesh fly (Sarcophaga crassipalpis) although hsp90 was suppressed. 67 Further studies showed that transcript levels of both hsp70a and hsp70b, one hsp60 member and four small hsps were upregulated in diapausing S. crassipalpis.…”

Section: Hsps In Insect Diapause and Cold-hardinessmentioning

confidence: 98%

Heat shock proteins and hypometabolism: adaptive strategy for proteome preservation

Storey¹,

Storey²

2011

RRB

View full text Add to dashboard Cite

Abstract:To survive under harsh environmental conditions many organisms retreat into hypometabolic states where metabolic rate may be reduced by 80% or more and energy use is reprioritized to emphasize key functions that sustain viability and provide cytoprotection. ATP-expensive activities, such as gene expression, protein turnover (synthesis and degradation), and the cell cycle, are largely shut down. As a consequence, mechanisms that stabilize the existing cellular proteome can become critical for long-term survival. Heat shock proteins (HSPs) are well-known for their actions as chaperones that act to fold new proteins or refold proteins that are damaged. Indeed, they are part of the "minimal stress proteome" that appears to be a ubiquitous response by all cells as they attempt, successfully or unsuccessfully, to deal with stress. The present review summarizes evidence that HSPs are also a conserved feature of natural animal hypometabolism including the phenomena of estivation, hibernation, diapause, cold-hardiness, anaerobiosis, and anhydrobiosis. That is, organisms that retreat into dormant or torpid states in anticipation that environmental conditions may become too difficult for normal life also integrate the use of HSPs to protect their proteome while hypometabolic. Multiple studies show a common upregulation of expression of hsp genes and/or HSP proteins prior to or during hypometabolism in organisms as diverse as ground squirrels, turtles, land snails, insects, and brine shrimp and in situations of both preprogrammed dormancies (eg, seasonal or life stage specific) and opportunistic hypometabolism (eg, triggered by desiccation or lack of oxygen). Hence, HSPs are not just a "shock" response that attempts to rescue cells from damaging stress but are a key protective strategy that is an integral component of natural states of torpor and dormancy.

show abstract

Temporal expression patterns of diapause-associated genes in flesh fly pupae from the onset of diapause through post-diapause quiescence

Cited by 124 publications

References 34 publications

Up-regulation of heat shock proteins is essential for cold survival during insect diapause

Up-regulation of heat shock proteins is essential for cold survival during insect diapause

Proteomic analysis of pre-diapause, diapause and post-diapause larvae of the wheat blossom midge, Sitodiplosis mosellana (Diptera: Cecidomyiidae)

Heat shock proteins and hypometabolism: adaptive strategy for proteome preservation

Contact Info

Product

Resources

About