BINDING PROPERTIES OF BOVINE OCULAR LENS ZETA-CRYSTALLIN TO RIGHT-HANDED B-DNA, LEFT-HANDED Z-DNA, AND SINGLE-STRANDED DNA

Bovine zeta-crystallin has the ability to bind with different DNAs. Initially, this protein was named regulatory factor 36 (Kanget al., 1985), but it has been shown to be an ocular lens zeta-crystallin (Jörnvallet al., 1993), which is considered an enzyme-crystallin (Rodakanakiet al., 1989). The enz...

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Bibliographic Details
Published in:Cell biology international 1998-03, Vol.22 (3), p.217-225
Main Authors: GAGNA, CLAUDE E, CHEN, JOHN H, KUO, HON-REEN, LAMBERT, W.CLARK
Format: Article
Language:English
Subjects:
Animals
B-DNA
Cattle
Crystallins - chemistry
Crystallins - metabolism
denatured single-stranded DNA
DNA - chemistry
DNA - metabolism
DNA unwinding (destabilizing) protein
DNA, Single-Stranded - chemistry
DNA, Single-Stranded - metabolism
double-stranded DNA
Enzyme-Linked Immunosorbent Assay
Kinetics
Lens, Crystalline - anatomy & histology
Lens, Crystalline - physiology
Nucleic Acid Conformation
Protein Binding
Z-DNA
zeta-crystallin
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Summary:Bovine zeta-crystallin has the ability to bind with different DNAs. Initially, this protein was named regulatory factor 36 (Kanget al., 1985), but it has been shown to be an ocular lens zeta-crystallin (Jörnvallet al., 1993), which is considered an enzyme-crystallin (Rodakanakiet al., 1989). The enzyme-linked immunosorbent assay (ELISA) was used to quantitate the binding of bovine zeta-crystallin to purified high molecular weight double-stranded (ds-) and single-stranded (ss-) DNA (bovine and synthetic DNA). ELISA quantitation was achieved by the addition of anti-zeta-crystallin antibodies to the DNA–zeta-crystallin complex, using a novel immunochemical avidin–biotin method. Zeta-crystallin shows much greater binding intensity for ss-DNA and for ds-Z-DNA than for ds-B-DNA. It also reacts slightly more with ds-Z-DNA than ss-DNA. Therefore, we speculate that zeta-crystallin may act as a transcriptional enhancer (outer lens cortex), possibly binding to Z-DNA regulatory elements within lens crystallin genes. It may also act to protect DNA from endogenous DNase activity and as a DNA unwinding (destabilizing) protein also involved with transcription, occurring in normal adult bovine lens nucleated secondary fiber cells.
ISSN:1065-6995
1095-8355
DOI:10.1006/cbir.1998.0243