Based upon DNA sequence analysis of the promoters from six gamma-crystallin genes (cryga-->crygf) a 36-bp DNA fragment was defined as 'Cryner' (cryg nested repeat). The presence of these repeats made this structure a candidate for DNA-protein interaction. The present experiments demonstrate interactions of lens proteins with the Cryner element from murine cryga, crygb, crygd and cryge. Additionally, DNA covering the sequence of about 30 nt between Cryner and the TATA-box of the murine crygb exhibits sequence-specific interactions with the bovine alpha-crystallin-containing fraction. The results confirm the hypothesis that the Cryner element is able to interact with lens proteins. It is noteworthy that this interaction is specific for the template strand of the DNA. The present model includes the possibility of sequence-dependent conformational changes leading to various DNA-protein complexes.