such as "Introduction", "Conclusion"..etc
The molecular structure of the protein, Mcm10, was published online
by the journal Structure on Dec. 9. Its discovery was a collaborative
effort by Brandt Eichman, assistant professor of biological sciences at
Vanderbilt University, and Walter Chazin, Chancellor's Professor of
Biochemistry and Physics at Vanderbilt, working with Anja
Katrin-Bielinsky at the University of Minnesota.
Currently, the process of DNA replication in eukaryote cells – cells
that have their genetic information contained in a nucleus – is a
"black box." Biologists know what goes in and what comes out but they
know very little about how the process actual works at the molecular
level. Because form causes function in the protein world, determining
the 3D structure of the 30-40 proteins that combine to form the
replisome is a necessary first step to figuring out the details of this
critical process and understanding how it can go wrong.
The structure of Mcm10 was determined using cells from the African
clawed frog (Xenopus laevis); the structures of analogous proteins in
human and other animal cells should be nearly identical, the
researchers maintain. The Mcm10 structure reveals a special feature,
called the OB-fold, that proteins use to interact with single-stranded
DNA and a series of three loops that the researchers believe are used
to clamp down on the DNA. The protein also contains a protrusion –
called a zinc finger because it is built around a zinc atom – that
proteins normally use to recognize specific double-stranded DNA
segments. In this case the zinc finger appears to be modified in a way
that allows it to detect generic DNA.
The researchers think that Mcm10 may play a role in positioning the
other proteins in the replisome onto the single DNA strand so that it
may be correctly read and duplicated, while acknowledging that they
have very little information about how it functions.
The research was funded in part by a grant from the National institutes of Health.
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