| dc.contributor |
Department of Biological Chemistry University of Michigan Medical School, Ann Arbor, Michigan 48109, USA |
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| dc.contributor |
Department of Microbiology and Immunology University of Michigan Medical School, Ann Arbor, Michigan 48109, USA |
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| dc.contributor |
Department of Microbiology and Immunology University of Michigan Medical School, Ann Arbor, Michigan 48109, USA |
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| dc.contributor |
Department of Microbiology and Immunology University of Michigan Medical School, Ann Arbor, Michigan 48109, USA |
|
| dc.contributor |
Department of Microbiology and Immunology University of Michigan Medical School, Ann Arbor, Michigan 48109, USA |
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| dc.contributor |
Department of Bacteriology University of Wisconsin, Madison, Wisconsin 53706, USA |
|
| dc.creator |
Landick, Robert C. |
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| dc.creator |
Vaughn, Vicki |
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| dc.creator |
Lau, Elizabeth T. |
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| dc.creator |
VanBogelen, Ruth A. |
|
| dc.creator |
Erickson, James W. |
|
| dc.creator |
Neidhardt, Frederick C. |
|
| dc.date |
2006-04-07T18:25:12Z |
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| dc.date |
2006-04-07T18:25:12Z |
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| dc.date |
1984-08 |
|
| dc.date.accessioned |
2022-05-19T13:30:07Z |
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| dc.date.available |
2022-05-19T13:30:07Z |
|
| dc.identifier |
Landick, Robert, Vaughn, Vicki, Lau, Elizabeth T., VanBogelen, Ruth A., Erickson, James W., Neidhardt, Frederick C. (1984/08)."Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor." Cell 38(1): 175-182. <http://hdl.handle.net/2027.42/24738> |
|
| dc.identifier |
http://www.sciencedirect.com/science/article/B6WSN-4C8GBFY-6C/2/65781c5c868fe0c02525b1ded67a16eb |
|
| dc.identifier |
http://www.ncbi.nlm.nih.gov/sites/entrez?cmd=retrieve&db=pubmed&list_uids=6088062&dopt=citation |
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| dc.identifier |
https://hdl.handle.net/2027.42/24738 |
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| dc.identifier |
6088062 |
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| dc.identifier |
http://dx.doi.org/10.1016/0092-8674(84)90538-5 |
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| dc.identifier |
Cell |
|
| dc.identifier.uri |
http://localhost:8080/xmlui/handle/CUHPOERS/117325 |
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| dc.description |
We have sequenced a cloned segment of E. coli chromosomal DNA that includes the heat shock regulatory gene htpR. This segment contains an 852 nucleotide open reading frame bounded by transcriptional and translational signals. Both in vivo and in vitro the cloned segment produces a single protein that migrates in gels with the cellular protein (F33.4) implicated as the htpR product. Properties of a cloned fragment of the coding sequence truncated at the promoter-distal end are consistent with this assignment. The htpR gene product appears homologous to the sigma factor of RNA polymerase, and the two proteins are predicted to have similar secondary structure. In addition, two regions of the predicted htpR product resemble protein-DNA contact points conserved in known DNA-binding proteins. |
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| dc.description |
Peer Reviewed |
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| dc.description |
http://deepblue.lib.umich.edu/bitstream/2027.42/24738/1/0000160.pdf |
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| dc.format |
1016948 bytes |
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| dc.format |
3118 bytes |
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| dc.format |
application/pdf |
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| dc.format |
text/plain |
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| dc.format |
application/pdf |
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| dc.language |
en_US |
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| dc.publisher |
Elsevier |
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| dc.rights |
IndexNoFollow |
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| dc.subject |
Molecular, Cellular and Developmental Biology |
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| dc.subject |
Science |
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| dc.subject |
Health Sciences |
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| dc.title |
Nucleotide sequence of the heat shock regulatory gene of E. coli suggests its protein product may be a transcription factor |
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| dc.type |
Article |
|