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J. Biol. Chem., Vol. 276, Issue 45, 41566-41575, November 9, 2001
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From the Departamento de Myxococcus xanthus transcriptional
factor CarD participates in carotenogenesis and fruiting body
formation. It is the only reported prokaryotic protein having adjacent
"AT-hook" DNA-binding and acidic regions characteristic of
eukaryotic high mobility group A (HMGA) proteins. The latter are small,
unstructured, nonhistone nuclear proteins that function as
architectural factors to remodel DNA and chromatin structure and
modulate various DNA binding activities. We find CarD to be
predominantly dimeric with two stable domains: (a) an
N-terminal domain of defined secondary and tertiary structure which is
absent in eukaryotic HMGA proteins; (b) a C-terminal domain
formed by the acidic and AT-hook segments and lacking defined structure. CarD, like HMGA proteins, binds specifically to the minor-groove of AT-rich DNA present in two appropriately spaced tracts.
As in HMGA proteins, casein kinase II can phosphorylate the CarD acidic
region, and this dramatically decreases the DNA binding affinity of
CarD. The acidic region, in addition to modulating DNA binding, confers
structural stability to CarD. We discuss how the structural and
functional plasticity arising from domain organization in CarD could be
linked to its role as a general transcriptional factor in M. xanthus.
Genética y
Microbiología and ¶ Area de Inmunología,
Universidad de Murcia, 30071 Murcia, Spain
Present address: Facultad de Ciencias Médicas de Sancti
Spiritus, Cuba.
**
To whom correspondence may be addressed. E-mail:
araujo@um.es.
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