Thymus satureioides and Origanum majorana essential oils improve the quality of Beni Arouss buck semen during storage at 4°C.

This study aims to investigate the effects of essential oils (EOs), extracted from Thymus satureioides (TS) and Origanum majorana (OM), on Beni Arouss buck semen quality stored in skimmed milk at 4°C. EOs were extracted by hydro-distillation, and the chemical compounds were determined. Ejaculates were collected from six Beni Arouss bucks, once a week for 10 weeks, and they were pooled, divided into five equal aliquots and diluted to 400 × 106 sperm/ml with skimmed milk supplemented with 0.01% of OM EO, 0.01% of TS EO, 0.05% of OM EO and 0.05% of TS EO. Non-supplemented skimmed milk was considered as a control. Semen motility, kinematic parameters, viability, abnormality, membrane integrity and lipid peroxidation were evaluated at 0, 4, 8, 24, 28, 32 and 48 hr of liquid storage at 4°C. The main EO components were carvacrol (31.7%), thymol (28.0%) and borneol (14.4%) for TS, and terpinene-4-ol (31.2%), γ-terpinene (17.4%) and α-terpinene (12.7%) for OM. The results highlighted a dose-dependent effect of TS and OM EOs on all semen quality parameters. 0.01% of both EOs had a beneficial effect on the sperm preservation stored at 4°C compared with control (p < .05) excepted for the straight-line velocity. The 0.05% EO addition had harmful effects during storage particularly for TS EO. In conclusion, 0.01% of TS and OM EOs are recommended to improve the Beni Arouss buck semen preservation at 4°C.

Effects of salt stress and rhizobial inoculation on growth and nitrogen fixation of three peanut cultivars.

Increasing soil salinity represents a major constraint for agriculture in arid and semi-arid lands, where mineral nitrogen (N) deficiency is also a frequent characteristic of soils. Biological N fixation by legumes may constitute a sustainable alternative to chemical fertilisation in salinity-affected areas, provided that adapted cultivars and inoculants are available. Here, the performance of three peanut cultivars nodulated with two different rhizobial strains that differ in their salt tolerance was evaluated under moderately saline water irrigation and compared with that of N-fertilised plants. Shoot weight was used as an indicator of yield. Under non-saline conditions, higher yields were obtained using N fertilisation rather than inoculation for all the varieties tested. However, under salt stress, the yield of inoculated plants became comparable to that of N-fertilised plants, with minor differences depending on the peanut cultivar and rhizobial strain. Our results indicate that N fixation might represent an economical, competitive and environmentally friendly choice with respect to mineral N fertilisation for peanut cultivation under moderate saline conditions.

Nucleolin forms a specific complex with a fragment of the viral (minus) strand of minute virus of mice DNA.

Nucleolin, a major nucleolar protein, forms a specific complex with the genome (a single-stranded DNA molecule of minus polarity) of parvovirus MVMp in vitro. By means of South-western blotting experiments, we mapped the binding site to a 222-nucleotide motif within the non-structural transcription unit, referred to as NUBE (nucleolin-binding element). The specificity of the interaction was confirmed by competitive gel retardation assays. DNaseI and nuclease S1 probing showed that NUBE folds into a secondary structure, in agreement with a computer-assisted conformational prediction. The whole NUBE may be necessary for the interaction with nucleolin, as suggested by the failure of NUBE subfragments to bind the protein and by the nuclease footprinting experiments. The present work extends the previously reported ability of nucleolin to form a specific complex with ribosomal RNA, to a defined DNA substrate. Considering the tropism of MVMp DNA replication for host cell nucleoli, these data raise the possibility that nucleolin may contribute to the regulation of the parvoviral life-cycle.

Identification of a transformation-sensitive nuclear protein from normal human fibroblasts that specifically interacts with minute virus of mice DNA and correlates with cell resistance to the parvovirus.

Normal human fibroblasts (MRC-5, KMS-6) were compared to transformed derivatives induced by SV40 (MRC-5V1) or gamma rays (KMST-6) for the expression of nuclear proteins that interact with the genome of minute virus of mice (MVMp), using the southwestern blot technique. A protein of 100-104 kDa apparent molecular weight was found to form a specific complex with MVMp DNA and to have an especially high affinity for the 3' terminal portion of the viral genome. This protein (p102) was differentially expressed by normal and transformed cells, i.e., its availability or DNA binding activity (or both) was much reduced in the transformants. A high level of p102 cosegregated with resistance to MVMp in cell hybrids between normal human and transformed mouse fibroblasts. Taken altogether these data suggest that the p102 protein may be a candidate for a transformation-sensitive cellular marker and for a negative regulator of parvovirus replication.