INVESTIGADORES
TROCHINE Andrea
artículos
Título:
Characterization of TcHMGB, a high mobility group B family member protein from Trypanosoma cruzi
Autor/es:
CRIBB P; PEROZZI M; VILLANOVA GV; TROCHINE A; SERRA E
Revista:
INTERNATIONAL JOURNAL FOR PARASITOLOGY
Editorial:
ELSEVIER SCI LTD
Referencias:
Lugar: Cairns; Año: 2011 vol. 41 p. 1149 - 1156
ISSN:
0020-7519
Resumen:
High mobility group B (HMGB) proteins are highly abundant non-histone
chromatin proteins that play important roles in the execution and
control of many nuclear functions. Based on homology searches, we
identified the coding sequence for the TcHMGB protein, an HMGB family
member from Trypanosoma cruzi. TcHMGB has two HMG box domains, similar
to mammalian HMGBs, but lacks the typical C-terminal acidic tail.
Instead, it contains a 110 amino acid long N-terminal domain. The TcHMGB
N-terminal domain is conserved between the TriTryp sequences (70-80%
similarity) and seems to be characteristic of kinetoplastid HMGBs.
Despite these differences, TcHMGB maintains HMG box architectural
functions: we demonstrated that the trypanosomatid HMGB binds distorted
DNA structures such as cruciform DNA in gel shift assays. TcHMGB is also
able to bend linear DNA as determined by T4 ligase circularization
assays, similar to other HMGB family members. Immunofluorescence and
western blot assays showed that TcHMGB is a nuclear protein expressed in
all life cycle stages. Protein levels, however, seem to vary throughout
the life cycle, which may be related to previously described changes in
heterochromatin distribution and transcription rates.