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From the Department of Ophthalmology, Mayo Clinic and Mayo Foundation, Rochester, Minnesota.
PURPOSE. To determine whether myocilin (MYOC; also referred to as TIGR) is present as a complex in human aqueous humor, whether part of the complex formation may be due to MYOC–MYOC interactions and to characterize the sites of interaction.
METHODS. Human aqueous humor was analyzed by using a gel filtration column for the identification of MYOC complexes. MYOC–MYOC interactions were studied with a yeast two-hybrid system. Expression of full-length and truncated MYOC proteins in AH109 yeast was analyzed for growth and color on minimal medium. Site-directed mutagenesis was used to selectively mutate eight leucine residues within the leucine zipper motif. In vitro transcription and translation was used to verify yeast two-hybrid analysis.
RESULTS. MYOC was found to be present in human aqueous humor as a complex ranging from 120 to 180 kDa. Expression of full-length MYOC in yeast as well as in vitro binding studies revealed that MYOC can interact with itself. MYOC–MYOC interactions occurred mainly within amino acids 117-166, a region containing a leucine zipper domain. Glycine substitution for selective leucine residues confirmed that MYOC–MYOC interactions occurred mainly within the leucine zipper domain.
CONCLUSIONS. MYOC is present in human aqueous humor, not as a monomer but as a complex. Part of this complex may form due to MYOC–MYOC interactions that take place mainly within the leucine zipper domain.
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