INVESTIGADORES
CANEPA Eduardo Tomas
artículos
Título:
Human p8 is a HMG_I/Y-like protein with DNA binding activity enhanced by phosphorylation
Autor/es:
JOSÉ A. ENCINAR; GUSTAVO V. MALLO; CYNTHIA MIZYRYCKI; LUCIANA E. GIONO; JOSÉ M. GONZÁLEZ-ROS; MANUEL RICO; EDUARDO T. CÁNEPA; SILVIA MORENO; JOSÉ L. NEIRA; JUAN LUCIO IOVANNA
Revista:
JOURNAL OF BIOLOGICAL CHEMISTRY
Editorial:
The American Society of Biochemistry and Molecular Biology Inc.
Referencias:
Lugar: Bethesda; Año: 2001 vol. 276 p. 2742 - 2751
ISSN:
0021-9258
Resumen:
We have studied the biochemical features, the conformational
preferences in solution, and the DNA binding
properties of human p8 (hp8), a nucleoprotein whose
expression is affected during acute pancreatitis. Biochemical
studies show that hp8 has properties of the
high mobility group proteins, HMG-I/Y. Structural studies
have been carried out by using circular dichroism
(near- and far-ultraviolet), Fourier transform infrared,
and NMR spectroscopies. All the biophysical probes indicate
that hp8 is monomeric (up to 1 mM concentration)
and partially unfolded in solution. The protein seems to
bind DNA weakly, as shown by electrophoretic gel shift
studies. On the other hand, hp8 is a substrate for protein
kinase A (PKA). The phosphorylated hp8 (PKAhp8) has a
higher content of secondary structure than the nonphosphorylated
protein, as concluded by Fourier transform
infrared studies. PKAhp8 binds DNA strongly, as
shown by the changes in circular dichroism spectra, and
gel shift analysis. Thus, although there is not a high
sequence homology with HMG-I/Y proteins, hp8 can be
considered as a HMG-I/Y-like protein.M concentration)
and partially unfolded in solution. The protein seems to
bind DNA weakly, as shown by electrophoretic gel shift
studies. On the other hand, hp8 is a substrate for protein
kinase A (PKA). The phosphorylated hp8 (PKAhp8) has a
higher content of secondary structure than the nonphosphorylated
protein, as concluded by Fourier transform
infrared studies. PKAhp8 binds DNA strongly, as
shown by the changes in circular dichroism spectra, and
gel shift analysis. Thus, although there is not a high
sequence homology with HMG-I/Y proteins, hp8 can be
considered as a HMG-I/Y-like protein.