The Drosophila melanogaster homologue of the hsp60 gene is encoded by the essential locus l(1)10Ac and is differentially expressed during fly development

Abstract

The hsp60 (heat-shock protein 60) gene family of molecular chaperones has been a subject of study in numerous systems due to its important role in the correct folding of non-native proteins in development as well as after heat-shock treatment. Here we present the characterization of the first Drosophila hsp60 homologue. Drosophila HSP60 is most closely related (72% identity across the entire protein sequence) to the mouse mitochondrial HSP60. Western blot experiments indicate that Drosophila HSP60 is enriched in the mitochondrial fraction. The distribution of HSP60 protein is dynamic during fly embryogenesis, suggesting that various cell types might have different HSP60 requirements. The molecular analysis of a P-element-induced mutation that affects the l(1)10Ac locus shows that the transposon is inserted in a 3-kb intron present in the hsp60 gene. By genetic rescue experiments we prove that Drosophila HSP60 is encoded by the essential locus l(1)10Ac opening the possibility for detailed genetic analysis of HSP60 functions in the fly.

Hsp60D is essential for caspase-mediated induced apoptosis in Drosophila melanogaster

“…Transcripts of Hsp60A and Hsp60C genes show low abundance in eye disc cells (Kozlova et al 1997;Sarkar and Lakhotia 2005) while Hsp60B is reported to express only in male germ cells (Timakov and Zhang 2001). However, information available in the databases on the expression of specific genes in different tissues of D. melanogaster (e.g., http://flybase.org or http://www.ncbi.…”

“…The Berkeley Drosophila Genome Project has reveled four Hsp60 genes, named as Hsp60A, Hsp60B, Hsp60C, and Hsp60D, respectively (Sarkar and Lakhotia 2005). Studies in our and other laboratories have shown that the Hsp60A, Hsp60B, and Hsp60C proteins have distinct functions in normal development (Kozlova et al 1997;Perezgasga et al 1999;Timakov and Zhang 2001;Lakhotia 2005, 2008;Sarkar et al 2006). …”

“…Scale bars represent 10 μm (bar in h is common for d-h and that in k is common for i-k) The above finding raised the possibility that the two antiHsp60 antibodies may recognize different Hsp60 forms present in D. melanogaster. It is known that Hsp60A is expressed ubiquitously but at low levels in most cell types of Drosophila (Kozlova et al 1997) while the Hsp60B is not expressed in any somatic cell (Timakov and Zhang 2001;Srivastava 2004). The Hsp60C is expressed ubiquitously, but at low levels, in most cells of larval eye discs (Sarkar and Lakhotia 2005).…”

Characterization and function analysis of Hsp60 and Hsp10 under different acute stresses in black tiger shrimp, Penaeus monodon

“…Hsp60 is able to substantially accelerate procaspase-3 maturation by different upstream activator caspases (Xanthoudakis et al 1999). The possible roles of Hsp60 in certain cellular processes, such as sperm cell differentiation, reproduction development, and environment stress response, have also been elucidated by other researches (Meinhardt et al 1995;Paranko et al 1996;Kozlova et al 1997;Neuer et al 2000;Qian et al 2012). Much of the research on organism protection under environmental stress in the last decades has examined the involvement of Hsp60 in multiple pathophysiological processes.…”

Molecular cloning and characterization of Cpn60 in the free-living nematode Plectus acuminatus

“…Using MitoProt II for Unix (Claros and Vincens 1996), it was possible to predict the mitochondrial signal sequence indicating, with a probability of P ϭ 0.96, that Cpn60 is indeed exported to the mitochondria (see Fig 1, panel A). The presence of a putative targeting signal that is responsible for the translocation into the mitochondrial matrix has also been reported in Cpn60 of Drosophila melanogaster (Kozlova et al 1997), Trypanosoma cruzi (Giambiagi-de Marval et al 1993), Culicoides variipennis (Abdallah et al 2000) and Paracentrotus lividus (Gianguzza et al 2000) and others. The deduced amino acid translation displays a considerable sequence identity (75%) and similarity (87%) to the Cpn60s from C elegans and C briggsae (Fig 1, panel B).…”