Distant homologs of anti-apoptotic factor HAX1 encode parvalbumin-like calcium binding proteins.

BMC Research Notes
Katarzyna KokoszyńskaLucjan S Wyrwicz

Abstract

Apoptosis is a highly ordered and orchestrated multiphase process controlled by the numerous cellular and extra-cellular signals, which executes the programmed cell death via release of cytochrome c alterations in calcium signaling, caspase-dependent limited proteolysis and DNA fragmentation. Besides the general modifiers of apoptosis, several tissue-specific regulators of this process were identified including HAX1 (HS-1 associated protein X-1) - an anti-apoptotic factor active in myeloid cells. Although HAX1 was the subject of various experimental studies, the mechanisms of its action and a functional link connected with the regulation of apoptosis still remains highly speculative. Here we provide the data which suggests that HAX1 may act as a regulator or as a sensor of calcium. On the basis of iterative similarity searches, we identified a set of distant homologs of HAX1 in insects. The applied fold recognition protocol gives us strong evidence that the distant insects' homologs of HAX1 are novel parvalbumin-like calcium binding proteins. Although the whole three EF-hands fold is not preserved in vertebrate our analysis suggests that there is an existence of a potential single EF-hand calcium binding site in HAX1. The molec...Continue Reading

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Methods Mentioned

BETA
two hybrid

Software Mentioned

SAM
3D
FFAS03
Discovery
PsiPred
Protein Structure Prediction MetaServer
Modeler
MetaBasic
INUB
PyMol

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