Provenance and tectonic significance of the Palaeoproterozoic metasedimentary successions of central and northern Madagascar

New detrital zircon U-Pb age data obtained from various quartzite units of three spatially separated supracrustal packages in central and northern Madagascar, show that these units were deposited between 1.8 and 0.8 Ga and have similar aged provenances. The distribution of detrital zircon ages indicates an overwhelming contribution of sources with ages between 2.5 and 1.8 Ga. Possible source rocks with an age of 2.5 Ga are present in abundance in the crustal segments (Antananarivo, Antongil and Masora Domains) either side of a purported Neoproterozoic suture ("Betsimisaraka Suture Zone"). Recently, possible source rocks for the 1.8 Ga age peak have been recognised in southern Madagascar. All three supracrustal successions, as well as the Archaean blocks onto which they were emplaced, are intruded by mid-Neoproterozoic magmatic suites placing a minimum age on their deposition. The similarities in detrital pattern, maximum and minimum age of deposition in the three successions, lend some support to a model in which all of Madagascar's Archaean blocks form a coherent crustal entity (the Greater Dharwar Craton), rather than an amalgamate of disparate crustal blocks brought together only during Neoproterozoic convergence. However, potential source terranes exist outside Madagascar and on either side of the Neoproterozoic sutures, so that a model including a Neoproterozoic suture in Madagascar cannot be dispelled outright

Functional evolution of scorpion venom peptides with an inhibitor cystine knot fold

The ICK (inhibitor cystine knot) defines a large superfamily of polypeptides with high structural stability and functional diversity. Here, we describe a new scorpion venom-derived K+ channel toxin (named lambda-MeuKTx-1) with an ICK fold through gene cloning, chemical synthesis, nuclear magnetic resonance spectroscopy, Ca2+ release measurements and electrophysiological recordings. lambda-MeuKTx-1 was found to adopt an ICK fold that contains a three-strand anti-parallel beta-sheet and a 3(10)-helix. Functionally, this peptide selectively inhibits the Drosophila Shaker K+ channel but is not capable of activating skeletal-type Ca2+ release channels/ryanodine receptors, which is remarkably different from the previously known scorpion venom ICK peptides. The removal of two C-terminal residues of lambda-MeuKTx-1 led to the loss of the inhibitory activity on the channel, whereas the C-terminal amidation resulted in the emergence of activity on four mammalian K+ channels accompanied by the loss of activity on the Shaker channel. A combination of structural and pharmacological data allows the recognition of three putative functional sites involved in channel blockade of lambda-MeuKTx-1. The presence of a functional dyad in lambda-MeuKTx-1 supports functional convergence among scorpion venom peptides with different folds. Furthermore, similarities in precursor organization, exon-intron structure, 3D-fold and function suggest that scorpion venom ICK-type K+ channel inhibitors and Ca2+ release channel activators share a common ancestor and their divergence occurs after speciation between buthidae and non-buthids. The structural and functional characterizations of the first scorpion venom ICK toxin with K+ channel-blocking activity sheds light on functionally divergent and convergent evolution of this conserved scaffold of ancient origin