Disease relevance of malG

• Sequence of gene malG in E. coli K12: homologies between integral membrane components from binding protein-dependent transport systems [1].
• Fusions were obtained by using either phage lambda TnphoA or by constructing in vitro fusions located randomly within the malG gene [2].

High impact information on malG

• Mutations in malG or malF that slightly affect or do not affect transport, determine a completely defective phenotype when present together [3].
• The products of the malF, malG, and malK genes form a membrane-associated complex that catalyzes the hydrolysis of ATP to provide energy for the transport event [4].
• The xylE gene was identified as a 1473-base pair open reading frame, located 373 base pairs downstream of malG, encoding a hydrophobic protein of Mr 53,607 [5].
• These results will be helpful for the interpretation of the phenotypes of mutants in malG [2].
• Fifteen mutations have been isolated in malG by random linker insertion mutagenesis [6].

Chemical compound and disease context of malG

• The malG gene encodes a hydrophobic cytoplasmic membrane protein which is required for the energy-dependent transport of maltose and maltodextrins in Escherichia coli [6].

Biological context of malG

• One short open reading frames orf1 (123 bp) and and the beginning of another one orf2 were localized after malG [7].

Anatomical context of malG

• Coexpression of malK, malF and malG in Escherichia coli resulted in the formation of a complex that could be coeluted from an affinity matrix after solubilization of membranes with dodecylmaltoside [8].

Associations of malG with chemical compounds

• To this end, single cysteine residues were introduced into each subunit at several positions and the respective malF and malG alleles were individually co-expressed with each of the malK alleles [9].
• Previously it was shown that alterations at residues glycine 13 and aspartate 14 of MBP can result in suppression of a malG mutant [10].

References