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Genetic dissection ...
Genetic dissection of a motility-associated c-di-GMP signalling protein of Pseudomonas putida
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- Österberg, Sofia (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)
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- Åberg, Anna (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)
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- Herrera Seitz, M. Karina (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)
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- Wolf-Watz, Magnus, 1971- (författare)
- Umeå universitet,Kemiska institutionen,Magnus Wolf-Watz
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- Shingler, Victoria (författare)
- Umeå universitet,Institutionen för molekylärbiologi (Teknisk-naturvetenskaplig fakultet)
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(creator_code:org_t)
- 2013-03-22
- 2013
- Engelska.
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Ingår i: Environmental Microbiology Reports. - Hoboken : Wiley-Blackwell. - 1758-2229. ; 5:4, s. 556-565
- Relaterad länk:
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https://urn.kb.se/re...
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https://doi.org/10.1...
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Abstract
Ämnesord
Stäng
- Lack of the Pseudomonas putidaPP2258 protein or its overexpression results in defective motility on solid media. The PP2258 protein is tripartite, possessing a PAS domain linked to two domains associated with turnover of c-di-GMP - a cyclic nucleotide that controls the switch between motile and sessile lifestyles. The second messenger c-di-GMP is produced by diguanylate cyclases and degraded by phosphodiesterases containing GGDEF and EAL or HD-GYP domains respectively. It is common for enzymes involved in c-di-GMP signalling to contain two domains with potentially opposing c-di-GMP turnover activities; however, usually one is degenerate and has been adopted to serve regulatory functions. Only a few proteins have previously been found to have dual enzymatic activities - being capable of both synthesizing and hydrolysing c-di-GMP. Here, using truncated and mutant derivatives of PP2258, we show that despite a lack of complete consensus in either the GGDEF or EAL motifs, the two c-di-GMP turnover domains can function independently of each other, and that the diguanylate cyclase activity is regulated by an inhibitory I-site within its GGDEF domain. Thus, motility-associated PP2258 can be added to the short list of bifunctional c-di-GMP signalling proteins.
Ämnesord
- NATURVETENSKAP -- Biologi -- Mikrobiologi (hsv//swe)
- NATURAL SCIENCES -- Biological Sciences -- Microbiology (hsv//eng)
Nyckelord
- diguanylate cyclase
- vibrio parahaemolyticus
- cyclic diguanylate
- allosteric control
- response regulator
- biofilm formation
- domain protein
- EAL domains
- Pilz domain
- phosphodiesterase
Publikations- och innehållstyp
- ref (ämneskategori)
- art (ämneskategori)
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