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Nucleic Acids Research, 1995, Vol. 23, No. 14 2654-2660
© 1995

MOLECULAR BIOLOGY

Single-stranded DNA binding proteins isolated from mouse brain recornize specific trinucleotide repeat sequences in vitro

Hiroko Yano-Yanagisawa, Yin Li, Hua Wang and Yoshinori Kohwi*

La Jolla Cancer Research Foundation La Jolla, CA 92037, USA

*To whom correspondence should be addressed

Received April 11, 1995. Accepted June 13, 1995.

Expansion of trinucleotide repeats (CAG)n and (CGG)n is found in genes responsible for certain human hereditary neurodegenerative diseases. By gel-mobility shift assay, we detected a single-stranded (AGC)n repeat-binding activity primarily In mouse brain extracts and very low or undetectable activity in other tissue extracts. Two (AGC)n-repeat binding proteins, with apparent molecular weights of 44 and 40 kDa, have been purified from mouse adult brain by a DNA affinity column and fast protein liquid chromatography. UVcross linking of radioiabeled (AGC)n repeats with crude brain extracts and with purified two proteins of 44 and 40 kDa produced identical doublet bands, indicating that these proteins are In fact responsible for the (AGC)n-binding activity in brain extracts. We designated these two proteins TRIP-1 for the 44 kDa protein and TRIP-2 for the 40 kDa protein, where TRIP represents trinucleotide repeat-binding protein. TRIP-1 and TRIP-2 bind to a specific subset of trinucleotide repeat sequences including (AGC)n, (AGT)n, (GGC)n, and (GGT)n repeats but not to various other trinucleotide repeats. A minimum of eight (AGC) trinucleotide repeating units is required for TRIP-1 and -2 recognition and binding. The (AGC)n repeat-binding activity increases In the brain after birth and reaches a plateau within 3 weeks. In the brain, TRIP-1 and TRIP-2 may alter the function of the genes containing the xpandedtrinucleotide repeats.


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