ArticleJournal of bacteriology1999
Structure-function study of MalF protein by random mutagenesis.
Article in Journal of bacteriology, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
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Who cites it
7 citing papers in PubMed.
- Binding Protein-Dependent Uptake of Maltose into Cells via an ATP-Binding Cassette Transporter.EcoSal Plus · 2010Article
- Transmembrane signaling in the maltose ABC transporter MalFGK2-E: periplasmic MalF-P2 loop communicates substrate availability to the ATP-bound MalK dimer.The Journal of biological chemistry · 2009Article
- The MalF P2 loop of the ATP-binding cassette transporter MalFGK2 from Escherichia coli and Salmonella enterica serovar typhimurium interacts with maltose binding protein (MalE) throughout the catalytic cycle.Journal of bacteriology · 2009Article
- Structure, function, and evolution of bacterial ATP-binding cassette systems.Microbiology and molecular biology reviews : MMBR · 2008Review
- Evolution of mal ABC transporter operons in the Thermococcales and Thermotogales.BMC evolutionary biology · 2008Article
- Characterization of transmembrane segments 3, 4, and 5 of MalF by mutational analysis.Journal of bacteriology · 2001Article
- The ArcB sensor kinase of Escherichia coli: genetic exploration of the transmembrane region.Journal of bacteriology · 2000Article
Corrections and comments
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Authors and funding
4 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
MalF is one of the two integral inner membrane proteins of the maltose-maltodextrin transport system. To identify functional regions in this protein, we characterized a collection of malF mutants obtained by random mutagenesis. We analyzed their growth on maltose and maltodextrins, the steady-state levels and subcellular localization of the mutant proteins, and the subcellular localization of MalK. Only 2 of the 21 MalF mutant proteins allowed growth on maltose and maltodextrins. Most mutations resulting in immunodetectable proteins mapped to hydrophilic domains, indicating that insertions affecting transmembrane segments gave rise to unstable or lethal proteins. All MalF mutant proteins, even those C-terminally truncated or with large N-terminal deletions, were inserted into the cytoplasmic membrane. Having identified mutations leading to reduced steady-state level, to partial mislocation, and/or to misfolding, we were able to assign to some regions of MalF a role in the assembly of the MalFGK2 complex and/or in the transport mechanism.
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