Disease relevance of malE

• We fused the wild-type Agrobacterium tumefaciens virG gene and the constitutive virGN54D allele to the malE gene of Escherichia coli, and studied the binding of MBP-VirG fusions to the autoregulated virG promoter [1].
• The malE gene lacking the DNA sequence that encodes the signal sequence was expressed in Escherichia coli [2].

High impact information on malE

• Escherichia coli strain MM18 cells containing malE-lacZ hybrid protein was reported to accumulate prolipoprotein when they were induced with maltose [Ito, K., Bassford, P. J. & Beckwith, J. (1981) Cell 24, 707-717] [3].
• The plasmid with the malE-pilR fusion, when introduced into a non-piliated pilR mutant strain of P. aeruginosa, restored piliation, indicating that the hybrid protein retains PilR function in vivo [4].
• The product of the malE-lacZ gene fusion was reported to compete with some proteins including outer membrane lipoprotein in the protein translocation across the Escherichia coli membrane [5].

Associations of malE with chemical compounds

• PilR was overproduced by fusing pilR to the gene for the maltose-binding protein (malE), yielding a MalE-PilR hybrid protein [4].

References