High impact information on KLF3

• In contrast, TEF-1 and a second SV40 enhancer binding protein, TEF-2, bind independently to templates containing the cognate motifs of both proteins (GT-I and either GT-IIC or Sph motifs) even though these motifs cooperate in enhancer activity in vivo [1].
• Basic Krüppel-like factor (BKLF) is a zinc finger protein that recognizes CACCC elements in DNA [2].
• Finally, we show that mutation of the CtBP NADH binding site impairs the ability of the proteins to dimerize and to associate with BKLF [3].
• Different but closely linked regions of BKLF mediate contact with CtBP2 and FHL3 [4].
• We show here that BKLF also recruits the four and a half LIM domain protein FHL3 [4].

Biological context of KLF3

• A novel element and a TEF-2-like element activate the major histocompatibility complex class II transactivator in B-lymphocytes [5].

Associations of KLF3 with chemical compounds

• Consistent with this result, we showed that mutation of the final histidine had only a modest effect on DNA binding in the context of the full three-finger DNA-binding domain of basic Krüppel-like factor [6].
• While the majority of these changes were silent, TEF-2 and TEF-3 differed from TEF-1 by having a lysine instead of a glutamate at amino acid position 41 [7].

References