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Protein family
HHA solution structure of hemolysin expression modulating protein hha from escherichia coli. ontario centre for structural proteomics target ec0308_1_72; northeast structural genomics target et88
Symbol HHA Pfam PF05321 InterPro IPR007985 SCOP2 1ir6 / SCOPe / SUPFAM
In molecular biology, the haemolysin expression modulating protein family is a family of proteins . This family consists of haemolysin expression modulating protein (Hha) from Escherichia coli and its enterobacterial homologues, such as YmoA from Yersinia enterocolitica , and RmoA encoded on the R100 plasmid . These proteins act as modulators of bacterial gene expression . Members of this family act in conjunction with members of the H-NS family, participating in the thermoregulation of different virulence factors and in plasmid transfer.[ 1] Hha, along with the chromatin -associated protein H-NS, is involved in the regulation of expression of the toxin alpha-haemolysin in response to osmolarity and temperature .[ 2] YmoA modulates the expression of various virulence factors, such as Yop proteins and YadA adhesin , in response to temperature. RmoA is a plasmid R100 modulator involved in plasmid transfer.[ 3] The HHA family of proteins display striking similarity to the oligomerisation domain of the H-NS proteins.
^ Madrid C, Nieto JM, Juarez A (February 2002). "Role of the Hha/YmoA family of proteins in the thermoregulation of the expression of virulence factors". Int. J. Med. Microbiol . 291 (6–7): 425–32. doi :10.1078/1438-4221-00149 . PMID 11890540 .
^ Nieto JM, Madrid C, Miquelay E, Parra JL, Rodriguez S, Juarez A (February 2002). "Evidence for direct protein-protein interaction between members of the enterobacterial Hha/YmoA and H-NS families of proteins" . J. Bacteriol . 184 (3): 629–35. doi :10.1128/jb.184.3.629-635.2002 . PMC 139531 . PMID 11790731 .
^ Nieto JM, Prenafeta A, Miquelay E, Torrades S, Juarez A (December 1998). "Sequence, identification and effect on conjugation of the rmoA gene of plasmid R100-1" . FEMS Microbiol. Lett . 169 (1): 59–66. doi :10.1111/j.1574-6968.1998.tb13299.x . PMID 9851035 .