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  • Genetics  (236)
  • Wiley-Blackwell  (236)
  • American Association for the Advancement of Science (AAAS)
  • Institute of Physics
  • Molecular Diversity Preservation International
  • Nature Publishing Group
  • 1990-1994  (236)
  • 1993  (236)
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Keywords
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  • Wiley-Blackwell  (236)
  • American Association for the Advancement of Science (AAAS)
  • Institute of Physics
  • Molecular Diversity Preservation International
  • Nature Publishing Group
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  • 1990-1994  (236)
Year
  • 1
    Electronic Resource
    Electronic Resource
    The independent stage-specific expression of the 18-kDa heat shock protein genes during microsporogenesis in Zea mays L (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 15-26 
    Details
    ISSN: 0192-253X
    Keywords: Heat shock protein ; maize ; mi-crosporogenesis ; gametogenesis ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The small (18-kDa) heat shock proteins (hsps) of maize are encoded by a complex multigene family. In a previous report, we described the genetic information from cDNAs encoding two different members of the family. In this communication, we report the isolation and characterization of cDNA and genomic clones encoding information for a third member of this hsp family (c/gMHSP18-1). DNA fragments containing nucleotide sequences common to, or specific for, each of these characterized 18-kDa genes were prepared and used as probes to assess the expression of these genes during microsporogenesis and development of the gametophyte in an inbred line of maize (Oh43). Our results demonstrate (1) that mRNA transcripts encoding the 18-kDa hsps are expressed and/or accumulate during microsporogenesis, and (2) that genes encoding two of the characterized 18-kDa hsps are expressed and/or accumulate independently, in a stage-specific manner during microsporogenesis. These observations imply that the stage-specific expression of particular 18-kDa hsp genes results from gene-specific regulation during microsporogenesis and gametophyte development rather than from an overall activation of the heat shock or stress response. © 1993Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140104
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  • 2
    Electronic Resource
    Electronic Resource
    Expression of endogenous and microinjected hsp 30 genes in early Xenopus laevis embryos (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 42-50 
    Details
    ISSN: 0192-253X
    Keywords: Development ; transcnption ; heat shock protein ; microinjection ; polymerase chain reaction ; Xenopus laevis ; mRNA ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the present study, we have examined the regulation of expression of a newly isolated member of the hsp 30 gene family, hsp 30C. Using RT-PCR, we found that this gene was first heat-inducible at the tailbud stage of development. We also examined the expression of two microinjected modified hsp 30C gene constructs in Xenopus embryos. One of the constructs had 404 bp of hsp 30C 5′-flanking region, whereas the other had 3.6 kb. Both gene constructs had 1 kb of 3′-flanking region. RT-PCR assays were employed to detect the expression of these microinjected genes. The presence of extensive 5′- and 3′-flanking regions of the hsp 30C gene did not confer proper developmental regulation, since heat-inducible expression of both of the microinjected constructs was detectable at the midblastula stage. The premature expression of the microinjected hsp 30 gene was not a result of high plasmid copy number or the presence of plasmid DNA sequences. These results suggest that the microinjected genes contain all the cis-acting DNA sequences required for correct heat-inducible regulation but do not contain the elements required for the proper regulation of hsp 30 gene expression during development. It is possible that regulatory elements controlling the developmental expression of the hsp30 genes may reside upstream or downstream of the entire cluster. © 1993Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140106
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  • 3
    Electronic Resource
    Electronic Resource
    Regulation of two different hsp70 transcript populations in steroid hormone-induced fungal development (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 6-14 
    Details
    ISSN: 0192-253X
    Keywords: hsp70 ; heat shock ; fungus ; steroid hormone ; secretion ; mycelial branching ; sexual differentiation ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: In the filamentous oomycete fungus Achlya, the differentiation of gamete bearing structures on vegetative hyphae of the male mating type, is induced by the Achlya steroid hormone, antheridiol. Among the several metabolically labeled intracellular proteins whose synthesis or accumulation is altered by hormone treatment are steroid-induced 85-kDa and 68- to 78-kDa proteins. The 85-kDa protein was previously shown to be the Achlya heat shock protein hsp85 [Brunt et al., 1990; Brunt and Silver, 1991], a component of the putative Achlya steroid hormone receptor. It was of interest to determine if the antheridiol-induced “70-kDa” proteins were hsp70-family heat shock proteins and if hormone treatment-induced changes in the level of hsp70 transcripts. Two different Achlya hsp70 genomic sequences were cloned and used to investigate these questions. The two hsp70 sequences recognized two different mycelial transcript populations, one of which was regulated also by decreased glucose. Of note, both of the two hsp70 transcript populations were found to be regulated by antheridiol. The hormone-induced chcnges in hsp70 transcript levels were temporally correlated with the onset of massive lateral hyphal branching and alterations in the pattern of secreted N-linked glycoproteins which occur in hormone-treated mycelia. To our kncwledge, this represents one of the first reports on changes in hsp70 proteins and transcripts during fungal differentiation. Our results may have implications for the role of heat shock proteins in hyphal branching and secretion in filamentous fungi and perhaps other cell types. © 1993Wiley-Liss, Inc. Inc.
    Additional Material: 3 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140103
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  • 4
    Electronic Resource
    Electronic Resource
    Characterization of two Maize HSP90 heat shock protein genes: Expression during heat shock, embryogenesis, and pollen development (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 27-41 
    Details
    ISSN: 0192-253X
    Keywords: Heat shock inducible promoters ; hsp90 ; Zea mays ; developmental expression ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have isolated two genes from Zea mays encoding proteins of 82 and 81 kD that are highly homologous to the Drosophila 83-kD heat shock protein gene and have analyzed the structure and pattern of expression of these two genes during heat shock and development. Southern blot analysis and hybrid select translations indicate that the highly homologous hsp82 and hsp81 genes are members of a small multigene family composed of at least two and perhaps three or more gene family members. The deduced amino acid sequence of these proteins based on the nucleotide sequence of the coding regions shows 64-88% amino acid homology to other hsp90 family genes from human, yeast, Drosophila, and Arabidopsis. The promoter regions of both the hsp82 and hsp81 genes contain several heat shock elements (HSEs), which are putative binding sites for heat shock transcription factor (HSF) commonly found in the promoters of other heat shock genes. Gene-specific oligonucleotide probes were synthesized and used to examine the mRNA expression patterns of the hsp81 and hsp82 genes during heat shock, embryogenesis, and pollen development. The hsp81 gene is only mildly heat inducible in leaf tissue, but is strongly expressed in the absence of heat shock during the premeiotic and meiotic prophase stages of pollen development and in embryos, as well as in heat-shocked embryos and tassels. The hsp82 gene shows strong heat inducibility at heat-shock temperatures (37-42°C) and in heat shocked embryos and tassels but is only weakly expressed in the absence of heat shock. Promoter-GUS reporter gene fusions made and analyzed by transient expression assays in Black Mexican Sweet (BMS) Maize protoplasts also indicate that the hsp82 and hsp81 are regulated differentially. The hsp82 promoter confers strong heat-inducible expression of the GUS reporter gene in heat-treated cells (60- to 80-fold over control levels), whereas the hsp81 promoter is only weakly heat inducible (5- to 10-fold over control levels). © 1993Wiley-Liss, Inc.
    Additional Material: 9 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140105
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  • 5
    Electronic Resource
    Electronic Resource
    Ferritin gene expression is developmentally regulated and induced by heat shock in sea urchin embryos (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 58-68 
    Details
    ISSN: 0192-253X
    Keywords: Ferritin ; heat shock ; development ; sea urchin ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: A 20-kD protein identified as a subunit of the iron-binding protein ferritin is present in S. purpuratus and L. pictus sea urchin embryos. The synthesis of the protein is stimulated by an elevation in temperature or by an increase in iron supply. The developmental expression of this protein and its regulation during normal development and upon heat shock was investigated. In L. pictus, ferritin is present in the unfertilized egg and, as determined by Western blot analysis, its concentration remains approximately constant after fertilization up to the gastrulc-pluteus stage; there is a small transient decrease in the level of the protein in the early blastula at a time coinciding with the first clear indication of its de novo synthesis. Northern blots reveal no cytoplasmic ferritin transcripts in the unfertilized egg, but there occurs a dramatic increase in the RNA level from the late morulaearly blastula stage (12-14 hr) to the mesenchyme blastula-early gastrula (25-30 hr) stage. This developmentally regulated increase in the constitutive concentration of ferritin RNA is correlatable with the normal onset of synthesis of the protein. The overall degree and nature of induction of ferritin by heat is dependent on the developmental stage: at 10-16 hr postfertilization heat shock elicits an increase in both the concentration of RNA and the synthesis of the protein; in hatched blastula (18 hr) and in later embryos heat shock increases ferritin synthesis, without a corresponding increase in the mRNA level. It appears that different mechanisms operate in the developing sea urchin embryo to regulate the expression of ferritin during normal development and on exposure to heat stress, one dependent on the concentration of ferritin transcripts and another operating at the level of translational control. © 1993Wiley-Liss, Inc.
    Additional Material: 7 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140108
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  • 6
    Electronic Resource
    Electronic Resource
    Heat shock gene expression and development. II. An overview of mammalian and avian developmental systems (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 87-91 
    Details
    ISSN: 0192-253X
    Keywords: Heat shock ; translation ; transcription ; development ; mRNA ; differentiation ; mammals ; birds ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140202
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  • 7
    Electronic Resource
    Electronic Resource
    Development and tissue-specific distribution of mouse small heat shock protein hsp25 (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 103-111 
    Details
    ISSN: 0192-253X
    Keywords: Mouse ; development ; small heat shock protein ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: We have investigated the developmental and tissue-specific distribution of the mouse small hsp25 by immunohistology using an antibody that specifically identifies hsp25. Our analysis shows that the relative amount of hsp25 increases during embryogenesis. Through days 13-20 of embryogenesis, hsp25 accumulation is predominant in the various muscle tissues, including the heart, the bladder, and the back muscles. hsp25 is detectable also in neurons of the spinal cord and the purkinje cells. Furthermore analysis of the closely related α, B-crystallin shows that in several tissues, including the bladder, the notochordal sheath and the eye lens both proteins are coexpressed. Our studies demonstrate that mammalian hsp25 accumulation is developmentally regulated during mouse embryogenesis and support the view of an important functional role of small heat shock proteins in normal cell metabolism. © 1993Wiley-Liss, Inc.
    Additional Material: 6 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140204
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  • 8
    Electronic Resource
    Electronic Resource
    HSP86 and HSP84 exhibit cellular specificity of expression and co-precipitate with an HSP70 family member in the murine testis (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 119-126 
    Details
    ISSN: 0192-253X
    Keywords: Spermatogenesis ; HSP90 proteins ; HSP70 proteins ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: This study extends to the protein level our previous observations, which had established the stage and cellular specificity of expression of hsp86 and hsp84 in the murine testis in the absence of exogenous stress. Immunoblot analysis was used to demonstrate that HSP86 protein was present throughout testicular development and that its levels increased with the appearance of differentiating germ cells. HSP86 was most abundant in the germ cell population and was present at significantly lower levels in the somatic cells. By contrast, the HSP84 protein was detected in the somatic cells of the testis rather than in germ cells. The steady-state levels of HSP86 and HSP84 paralleled the pattern of the expression of their respective mRNAs, suggesting that regulation at the level of translation was not a major mechanism controlling hsp90 gene expression in testicular cells. Immunoprecipitation analysis revealed that a 70-kDa protein coprecipitated with the HSP86/HSP84 proteins in testicular homogenates. This protein was identified as an HSP70 family member by immunoblot analysis, suggesting that HSP70 and HSP90 family members interact in testicular cells. © 1993Wiley-Liss, Inc.
    Additional Material: 4 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140206
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  • 9
    Electronic Resource
    Electronic Resource
    Lack of concordance between heat shock proteins and the development of tolerance to teratogen-induced neural tube defects (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 137-147 
    Details
    ISSN: 0192-253X
    Keywords: Heat-shock proteins ; teratogenicity, tolerance and cross-tolerance ; neural tube defects ; gene expression ; In situ transcription ; Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Notes: The present study was undertaken to examine the role of heat shock response in the development of tolerance and cross-tolerance in an in vivo murine model of teratogen-induced neural tube defects. The experimental paradigm designed to address this question was to utilize inbred mouse strains that differed in their sensitivity to hyperthermia and valproic acid induced neural tube defects, subjecting the dams to subteratogenic pretreatments with either heat or valproic acid at two different timepoints during development prior to the administration of the teratogenic insult. A statistically significant reduction in the frequency of neural tube defects and/or embryolethality following a pretreatment in dams subsequently exposed to a teratogenic treatment was considered evidence for the induction of tolerance. This was observed in the SWV embryos exposed to the 38°C pretreatment at 8:06 and to embryos exposed to either pretreatment temperature at 8:10 priorto a teratogenic heat shock at 8:12. In the LM/Bc embryos, only the 41°C pretreatment at 8:06 induced thermotolerance. There was no evidence of tolerance induced in either mouse strain using valproic acid. On the other hand, cross-tolerance was clearly demonstrated in this study, with a low temperature (41°C) pretreatment successfully protecting SWV fetuses from a subsequent teratogenic treatment with valproic acid, while valproic acid (200 mg/kg) was effective in reducing the risk of hyperthermia-induced neural tube defects in the LM/Bc fetuses. In all instances, tolerance was induced in the absence of significant induction of hsp synthesis. The lack ofconcordance between hsps and thermotolerance suggests that some other factor(s) is involved in conferring thermotolerance on developing murine embryos. © 1993 Wiley-Liss, Inc.
    Additional Material: 2 Ill.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140208
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  • 10
    Electronic Resource
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    Erratum (1993)
    Chichester [u.a.] : Wiley-Blackwell
    Developmental Genetics 14 (1993), S. 249-249 
    Details
    ISSN: 0192-253X
    Keywords: Life and Medical Sciences ; Genetics
    Source: Wiley InterScience Backfile Collection 1832-2000
    Topics: Biology
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1002/dvg.1020140311
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