Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein
Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C...
Ausführliche Beschreibung
Gespeichert in:
| Autor*in: |
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| Format: |
E-Artikel |
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| Sprache: |
Englisch |
| Erschienen: |
1993 |
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| Umfang: |
8 |
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| Reproduktion: |
Springer Online Journal Archives 1860-2002 |
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| Übergeordnetes Werk: |
in: Molecular genetics and genomics - 1908, 239(1993) vom: Jan./Feb., Seite 273-280 |
| Übergeordnetes Werk: |
volume:239 ; year:1993 ; month:01/02 ; pages:273-280 ; extent:8 |
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| 520 | |a Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. | ||
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(DE-627)NLEJ205446531 DE-627 ger DE-627 rakwb eng Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein 1993 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. Springer Online Journal Archives 1860-2002 Russo, Patrick oth Simonen, Marjo oth Uimari, Anne oth Teesalu, Tambet oth Makarow, Marja oth in Molecular genetics and genomics 1908 239(1993) vom: Jan./Feb., Seite 273-280 (DE-627)NLEJ188991441 (DE-600)1462070-4 1617-4623 nnns volume:239 year:1993 month:01/02 pages:273-280 extent:8 http://dx.doi.org/10.1007/BF00281628 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 239 1993 1/2 273-280 8 |
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(DE-627)NLEJ205446531 DE-627 ger DE-627 rakwb eng Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein 1993 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. Springer Online Journal Archives 1860-2002 Russo, Patrick oth Simonen, Marjo oth Uimari, Anne oth Teesalu, Tambet oth Makarow, Marja oth in Molecular genetics and genomics 1908 239(1993) vom: Jan./Feb., Seite 273-280 (DE-627)NLEJ188991441 (DE-600)1462070-4 1617-4623 nnns volume:239 year:1993 month:01/02 pages:273-280 extent:8 http://dx.doi.org/10.1007/BF00281628 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 239 1993 1/2 273-280 8 |
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(DE-627)NLEJ205446531 DE-627 ger DE-627 rakwb eng Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein 1993 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. Springer Online Journal Archives 1860-2002 Russo, Patrick oth Simonen, Marjo oth Uimari, Anne oth Teesalu, Tambet oth Makarow, Marja oth in Molecular genetics and genomics 1908 239(1993) vom: Jan./Feb., Seite 273-280 (DE-627)NLEJ188991441 (DE-600)1462070-4 1617-4623 nnns volume:239 year:1993 month:01/02 pages:273-280 extent:8 http://dx.doi.org/10.1007/BF00281628 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 239 1993 1/2 273-280 8 |
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(DE-627)NLEJ205446531 DE-627 ger DE-627 rakwb eng Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein 1993 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. Springer Online Journal Archives 1860-2002 Russo, Patrick oth Simonen, Marjo oth Uimari, Anne oth Teesalu, Tambet oth Makarow, Marja oth in Molecular genetics and genomics 1908 239(1993) vom: Jan./Feb., Seite 273-280 (DE-627)NLEJ188991441 (DE-600)1462070-4 1617-4623 nnns volume:239 year:1993 month:01/02 pages:273-280 extent:8 http://dx.doi.org/10.1007/BF00281628 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 239 1993 1/2 273-280 8 |
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(DE-627)NLEJ205446531 DE-627 ger DE-627 rakwb eng Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein 1993 8 nicht spezifiziert zzz rdacontent nicht spezifiziert z rdamedia nicht spezifiziert zu rdacarrier Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. Springer Online Journal Archives 1860-2002 Russo, Patrick oth Simonen, Marjo oth Uimari, Anne oth Teesalu, Tambet oth Makarow, Marja oth in Molecular genetics and genomics 1908 239(1993) vom: Jan./Feb., Seite 273-280 (DE-627)NLEJ188991441 (DE-600)1462070-4 1617-4623 nnns volume:239 year:1993 month:01/02 pages:273-280 extent:8 http://dx.doi.org/10.1007/BF00281628 GBV_USEFLAG_U ZDB-1-SOJ GBV_NL_ARTICLE AR 239 1993 1/2 273-280 8 |
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dual regulation by heat and nutrient stress of the yeast hsp150 gene encoding a secretory glycoprotein |
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Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein |
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Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. |
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Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. |
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Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE. |
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<?xml version="1.0" encoding="UTF-8"?><collection xmlns="http://www.loc.gov/MARC21/slim"><record><leader>01000caa a22002652 4500</leader><controlfield tag="001">NLEJ205446531</controlfield><controlfield tag="003">DE-627</controlfield><controlfield tag="005">20210706175354.0</controlfield><controlfield tag="007">cr uuu---uuuuu</controlfield><controlfield tag="008">070528s1993 xx |||||o 00| ||eng c</controlfield><datafield tag="035" ind1=" " ind2=" "><subfield code="a">(DE-627)NLEJ205446531</subfield></datafield><datafield tag="040" ind1=" " ind2=" "><subfield code="a">DE-627</subfield><subfield code="b">ger</subfield><subfield code="c">DE-627</subfield><subfield code="e">rakwb</subfield></datafield><datafield tag="041" ind1=" " ind2=" "><subfield code="a">eng</subfield></datafield><datafield tag="245" ind1="1" ind2="0"><subfield code="a">Dual regulation by heat and nutrient stress of the yeast HSP150 gene encoding a secretory glycoprotein</subfield></datafield><datafield tag="264" ind1=" " ind2="1"><subfield code="c">1993</subfield></datafield><datafield tag="300" ind1=" " ind2=" "><subfield code="a">8</subfield></datafield><datafield tag="336" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zzz</subfield><subfield code="2">rdacontent</subfield></datafield><datafield tag="337" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">z</subfield><subfield code="2">rdamedia</subfield></datafield><datafield tag="338" ind1=" " ind2=" "><subfield code="a">nicht spezifiziert</subfield><subfield code="b">zu</subfield><subfield code="2">rdacarrier</subfield></datafield><datafield tag="520" ind1=" " ind2=" "><subfield code="a">Abstract We have cloned and characterized the HSP150 gene of Saccharomyces cerevisiae, which encodes a glycoprotein (hsp150) that is secreted into the growth medium. Unexpectedly, the HSP150 gene was found to be regulated by heat shock and nitrogen starvation. Shifting the cells from 24° C to 37° C resulted in an abrupt increase in the steady-state level of the HSP150 mRNA, and de novo synthesized hsp150 protein. Returning the cells to 24° C caused a rapid decrease in mRNA and protein synthesis to basal levels. The HSP150 5′-flanking region contains several heat shock element-like sequences (HSE). To study the function of these sequences, a strain bearing a disrupted copy of the HSP150 gene was transformed with plasmids in which the coding region of HSP150, or a HSP150-lacZ fusion gene, was preceded by 5′ deletion derivatives of the HSP150 promoter. Site-directed mutagenesis of one HSE-like element, located between the TATA box and transcription initiation sites, abolished heat activation of transcription. In addition to heat shock, the HSP150 gene is regulated by the availability of nutrients in the growth medium. The HSP150 mRNA level was increased by nitrogen limitation at 24° C, even when under the control of a HSP150 promoter region of 137 by carrying the mutagenized HSE.</subfield></datafield><datafield tag="533" ind1=" " ind2=" "><subfield code="f">Springer Online Journal Archives 1860-2002</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Russo, Patrick</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Simonen, Marjo</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Uimari, Anne</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Teesalu, Tambet</subfield><subfield code="4">oth</subfield></datafield><datafield tag="700" ind1="1" ind2=" "><subfield code="a">Makarow, Marja</subfield><subfield code="4">oth</subfield></datafield><datafield tag="773" ind1="0" ind2="8"><subfield code="i">in</subfield><subfield code="t">Molecular genetics and genomics</subfield><subfield code="d">1908</subfield><subfield code="g">239(1993) vom: Jan./Feb., Seite 273-280</subfield><subfield code="w">(DE-627)NLEJ188991441</subfield><subfield code="w">(DE-600)1462070-4</subfield><subfield code="x">1617-4623</subfield><subfield code="7">nnns</subfield></datafield><datafield tag="773" ind1="1" ind2="8"><subfield code="g">volume:239</subfield><subfield code="g">year:1993</subfield><subfield code="g">month:01/02</subfield><subfield code="g">pages:273-280</subfield><subfield code="g">extent:8</subfield></datafield><datafield tag="856" ind1="4" ind2="0"><subfield code="u">http://dx.doi.org/10.1007/BF00281628</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_USEFLAG_U</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">ZDB-1-SOJ</subfield></datafield><datafield tag="912" ind1=" " ind2=" "><subfield code="a">GBV_NL_ARTICLE</subfield></datafield><datafield tag="951" ind1=" " ind2=" "><subfield code="a">AR</subfield></datafield><datafield tag="952" ind1=" " ind2=" "><subfield code="d">239</subfield><subfield code="j">1993</subfield><subfield code="c">1/2</subfield><subfield code="h">273-280</subfield><subfield code="g">8</subfield></datafield></record></collection>
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7.400717 |