IIB   20738
INSTITUTO DE INVESTIGACIONES BIOLOGICAS
Unidad Ejecutora - UE
congresos y reuniones científicas
Título:
P400C, a protein containing an Ubiquitin-like domain from Natrialba magadii. In silico characterization
Autor/es:
ORDÓÑEZ, M.V.; NERCESSIAN, D.; CONDE, R.D.
Lugar:
Puerto Madryn
Reunión:
Congreso; XLVI Reunión Anual de la Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB); 2010
Institución organizadora:
Sociedad Argentina de Investigación en Bioquímica y Biología Molecular (SAIB)
Resumen:
Ubiquitin-like proteins and Ubiquitin-like
domain containing proteins have been found in both eukaryotes and prokaryotes.
They belong to the β-grasp fold characterized by 4-5 antiparallel β-sheets with
a middle α-helix region.
Searching for the presence of Ubls in
halophilic archaea, we previously
found by both in silico and FTIR analysis
that P400, a polypeptide from Natrialba
magadii, displays structural homology with Ubiquitin-like proteins. The aim
of this work was to characterize the Nmag_2608 protein that includes P400. This conserved hypothetical protein of
262 amino acids is part of a group of orthologs from different halophilic
archaea with no significant sequence likeness to known proteins. Secondary
folding prediction showed that they are mainly composed by β-sheets. Also, bioinformatics
analysis predicted that Nmag_2608 and most of its orthologs contain a signal
peptide with a conserved LIPOBOX motif found in bacterial lipoproteins. Lastly,
expression of Nmag_2608 in N. magadii
cells allowed to detect, only in the stationary phase of growth, a 1.4 kbps
transcript. All together, these results suggest that P400 is an Ubiquitin-like
domain inside a membrane anchored protein expressed in N. magadii at late stages of growth. Supported
by UNMdP and CONICET.