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## Abstract **Background:** Members of the Maf family, including L‐Maf, MafB and c‐Maf, are ‘basic region/leucine zipper’ (bZIP) transcription factors. Maf proteins contain a highly conserved acidic transactivation domain (AD), and a bZIP region that mediates DNA‐binding activity. The hinge region between AD and bZIP varies considerably in length between different proteins. Recent studies reveal that L‐Maf, c‐Maf and MafB play key roles in vertebrate lens development. **Results:** We investigated the transactivation activity of individual factors in culture cells to analyse their specific functions. In transient transfection assays with a reporter gene containing Maf responsive elements, MafB and c‐Maf activated higher levels of the reporter gene than L‐Maf. However, L‐Maf transactivated the αA‐crystallin promoter as effectively as MafB and c‐Maf, and induced the expression of the endogenous δ‐crystallin gene more efficiently than the other two proteins. Domain‐swapping experiments reveal that the bZIP region of MafB takes part in strong transcriptional activity, while the acidic and hinge regions (AH) of c‐Maf collectively serve as a strong transactivation domain. The AH region of

Author

Tomonori Yoshida; Kunio Yasuda

Publisher

John Wiley and Sons; Wiley (Blackwell Publishing); Blackwell Publishing Inc.; Wiley (ISSN 1356-9597)

Published

2002

Language

EN