The complete mitochondrial genome of the terrestrial snail (O.F. Müller, 1774) (Gastropoda, Eupulmonata, Hygromiidae).

The mitochondrial genome of is the first complete mitochondrial sequence described for the pulmonate snail genus and for the family Hygromiidae. The identified mitogenome has a length of 13,894 bp and encodes 13 proteins, 22 tRNAs, and two rRNAs. A phylogenetic analysis of available mitogenomes from representatives of helicoid families shows a sister group relationship of Hygromiidae and Geomitridae, which have been recently recognised as separate families.

Redescription of (De Stefani, 1879), a species endemic to the central Apennines, Italy (Gastropoda, Eupulmonata, Hygromiidae) by an integrative molecular and morphological approach.

Specimens obtained from ten populations of a species from the central Apennines were compared with six molecular lineages of s. l. (CAN-1, CAN-2, CAN-3, CAN-4, CAN-5, CAN-6) and two other species ( and ), treated as outgroup, by molecular (nucleotide sequences of two mitochondrial COI and 16S rDNA as well as two nuclear ITS2 and H3 gene fragments) and morphological (shell and genital anatomy) analysis.

Arabidopsis thaliana egy2 mutants display altered expression level of genes encoding crucial photosystem II proteins.

EGY2 is a zinc-containing, intramembrane protease located in the thylakoid membrane. It is considered to be involved in the regulated intramembrane proteolysis - a mechanism leading to activation of membrane-anchored transcription factors through proteolytic cleavage, which causes them to be released from the membrane. The physiological functions of EGY2 in chloroplasts remains poorly understood.

Putative new groups of invertebrate water channels based on the snail Helix pomatia L. (Helicidae) MIP protein identification and phylogenetic analysis.

Water channel proteins, classified as a family of Membrane Intrinsic Proteins (MIPs) superfamily, enable rapid movement of water and small uncharged molecules through biological membranes. Although water channel proteins are required in several important processes characteristic for the animals, such as osmoregulation, mucus secretion, or defense against desiccation, molluscs, until now, have been very poorly explored in this aspect. Therefore, we decided to study MIPs in Helix pomatia L.

Molecular identification of first putative aquaporins in snails.

Aquaporins (AQPs), also known as water channel proteins, are members of a large protein family termed Major Intrinsic Proteins (MIP). The mammalian AQPs have been most comprehensively described, while knowledge about AQPs in invertebrates is limited mainly to insects. Not a single AQP protein has been described in snails to date.