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  Adenylate kinases from thermosensitive Escherichia coli strains

Haase, G. H. W., Brune, M., Reinstein, J., Pai, E. F., Pingoud, A., & Wittinghofer, A. (1989). Adenylate kinases from thermosensitive Escherichia coli strains. Journal of Molecular Biology (London), 207(1), 151-162. doi:10.1016/0022-2836(89)90446-4.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-0019-ADAC-6 Version Permalink: http://hdl.handle.net/21.11116/0000-0002-6A0B-C
Genre: Journal Article

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JMolBiol_207_1989_151.pdf (Any fulltext), 3MB
 
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 Creators:
Haase, Georg H. W., Author
Brune, Martin, Author
Reinstein, Jochen1, Author              
Pai, Emil F., Author
Pingoud, Alfred, Author
Wittinghofer, Alfred2, Author              
Affiliations:
1Department of Biomolecular Mechanisms, Max Planck Institute for Medical Research, Max Planck Society, ou_1497700              
2Emeritus Group Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_1497712              

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 Abstract: The adk genes from several thermosensitive (ts) mutants of Escherichia coli were cloned and sequenced. The mutations responsible for the thermolability of the gene product, the enzyme adenylate kinase, were established. From five independently isolated strains analysed, two contain a CCG to TCG transition changing proline 87 to serine (P87S), another two have a TCT to TTT transition that mutates serine 129 to phenylalanine (S129F), and the last one was found not to contain a mutation in the adk gene. Overproducing strains were constructed that contain ts genes in the genome as well as in the plasmids. These strains grow at high temperature, although much slower than wild-type. Most probably, the high rate of synthesis of adenylate kinase compensates for the destruction of the thermolabile protein by the elevated temperature. Mutated proteins were purified. The P87S but not the S129F mutation was found to cause thermosensitivity of the adenylate kinase reaction. Revertants of thermosensitivity were isolated and the nature of the mutation was determined by the RNase digestion method of RNA-DNA hybrids and by DNA sequencing. The revertants of the P87S mutation regained the wild-type sequence, whereas the revertants of the S129F strain retained the original mutation in the adenylate kinase gene. These results are discussed in the light of the three-dimensional structure of the enzyme and the possible role of adenylate kinase in phospholipid synthesis.

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Language(s): eng - English
 Dates: 1988-12-021988-05-161989-05-05
 Publication Status: Published in print
 Pages: 12
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 Rev. Type: Peer
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Title: Journal of Molecular Biology (London)
  Other : J Mol Biol
Source Genre: Journal
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Publ. Info: London : Academic Press
Pages: - Volume / Issue: 207 (1) Sequence Number: - Start / End Page: 151 - 162 Identifier: ISSN: 0022-2836
CoNE: https://pure.mpg.de/cone/journals/resource/954922646042