TY - JOUR
T1 - Identification of nuclear factor δEF1 and its binding site essential for lens-specific activity of the δ1-crystallin enhancer
AU - Funahashi, Jun ichi
AU - Kamachi, Yusuke
AU - Goto, Koji
AU - Kondoh, Hisato
N1 - Funding Information:
K.Goto was the recipient of a Fellowship from the Japan Society for the Promotion of Science for Japan Junior Scientists. This work was supported by grants from the Ministry of Education, Science and Culture of Japan to H.K. and to K.G., and from the Science and Technology Agency of Japan to H.K.
PY - 1991/7/11
Y1 - 1991/7/11
N2 - The lens-specific reglatory element of the δ1-crystallin enhancer lies within the core segment (Goto et al., (1990) Mol. Cell. Biol. 10, 935-964). The element was allocated within the 55 bp long HN fragment of the core. Block-wise base substitutions were introduced to the 55 bp and their effect on the enhancer activity of the multimers in lens cells was examined. By base sequence alteration of either of the contiguous blocks 5 and 6, with their original sequence of TTGCT and C-ACCT, respectively, enhancer activity was totally lost. A lens nuclear factor δEF1 was found which bound specifically to the base sequences defined by the blocks. DNA binding activity very similar to δEF1 was also found in extracts of tissues other than lens, suggesting that δEFI participates in lens-specific regulation through tissue-dependent modification or interaction with other factors.
AB - The lens-specific reglatory element of the δ1-crystallin enhancer lies within the core segment (Goto et al., (1990) Mol. Cell. Biol. 10, 935-964). The element was allocated within the 55 bp long HN fragment of the core. Block-wise base substitutions were introduced to the 55 bp and their effect on the enhancer activity of the multimers in lens cells was examined. By base sequence alteration of either of the contiguous blocks 5 and 6, with their original sequence of TTGCT and C-ACCT, respectively, enhancer activity was totally lost. A lens nuclear factor δEF1 was found which bound specifically to the base sequences defined by the blocks. DNA binding activity very similar to δEF1 was also found in extracts of tissues other than lens, suggesting that δEFI participates in lens-specific regulation through tissue-dependent modification or interaction with other factors.
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U2 - 10.1093/nar/19.13.3543
DO - 10.1093/nar/19.13.3543
M3 - Article
C2 - 1852604
AN - SCOPUS:0025781194
SN - 0305-1048
VL - 19
SP - 3543
EP - 3547
JO - Nucleic Acids Research
JF - Nucleic Acids Research
IS - 13
ER -