The complete mitochondrial genome of the domestic red deer (Cervus elaphus) of New Zealand and its phylogenic position within the family Cervidae

We determined the complete nucleotide sequence of the mitochondrial genome of the semidomestic red deer (Cervus elaphus) of New Zealand. The genome was 16 357 bp long and contained 13 protein‐coding genes, 12SrRNA, 16SrRNA, 22 tRNAs and a D‐loop as found in other mammals. Database homology searches showed that the mitochondrial DNA (mtDNA) sequence from the New Zealand semidomestic deer was similar to partial mtDNA sequences from the European, Norwegian (C. e. atlanticus) and Spanish red deer (C. e. hispanicus). Phylogenetic analysis of the mitochondrial protein‐coding regions revealed two well‐defined monophyletic clades in subfamilies Cervinae and Muntiacinae. However, red deer and Sika deer were not found to be close relatives. The analysis did identify the red deer as a sister taxon of a Samber/Sika deer clade, although it was more closely related to the Samber than the Sika group.     

Expression analysis of the type I keratin protein keratin 33A in goat coat hair

The coat of a goat, like that of many mammalian species, consists of an outer coat of coarse hairs and an under coat of fine, downy hairs. The coarse guard hairs are produced by primary follicles and the finer cashmere hairs by secondary follicles. We previously reported that hair keratins are components of cashmere hair, and proteomic analysis revealed that their expression is elevated in winter coat hair. To determine detailed characterization, we have cloned keratin 33A gene, a major highly expressed keratin in winter, and then analyzed the expression of goat hair coat. By Western analysis, we detected that keratin 33A protein is expressed only in hair coat among the various goat tissues. Moreover, the expression level in winter has increased in cashmere high‐producing Korean native breed, whereas the expression levels between summer and winter had not changed in cashmere low‐producing Saanen. In addition, by immunohistochemistry we determined that keratin 33A is localized in the major cortex portion of cashmere fiber. These results confirm that keratin 33A is a structural protein of goat cashmere hair fiber.     

Twenty-three years of stand dynamics in an old-growth Chamaecyparis forest in central Japan

Structures and dynamics of old-growth coniferous stands are affected by several types of disturbances including typhoons. We report the forest dynamics of four old-growth Chamaecyparis stands in central Japan that differ in the disturbance history of typhoons over a period of 23 years. The stem number, basal area and mortality were examined. In a predominant stand of C. obtusa (Sieb. et Zucc.) Endl., 24 % of the C. obtusa canopy trees died, mainly as a result of the severe damage of a strong typhoon that caused a single tree-fall gap and the following gap enlargements. In this stand, the total basal area decreased to 76.5 % of the initial value, although the mortality declined in recent years. In contrast, the other three stands decreased only slightly in the stem numbers (0.0–5.6 %) and increased in the basal areas of C. obtusa canopy trees. It is confirmed that the stand-level ingrowths of 300-year-old C. obtusa canopy trees could contribute to the increase in the stock of each stand. Our results support an idea that the dynamics of old-growth Chamaecyparis forests were greatly affected by typhoons. The stand structures will be gradually changed (with the processes of gap dynamics) and C. obtusa will continue to be dominant, potentially over hundreds of years.     

Analysis of mitochondrial DNA protein-coding region in the Yeso Sika deer (Cervus nippon yesoensis)

In the present study, mitochondrial DNA sequences of the Yeso Sika deer (Cervus nippon yesoensis) were studied. Specifically, protein‐coding genes as mitochondrial NADH dehydrogenase subunits (ND1, ND2, ND3, ND4L, ND4, ND5 and ND6), cytochrome c oxidase subunits (CO I and CO III), ATP synthase subunits (ATPase8 and ATPase6) and cytochrome b. Also, phylogenetic analyses on eight mammalian species were performed, including the Muntjac deer (Muntiacus reevesi). The rate of amino‐acid substitution was lowest (3.74%) between Yeso Sika deer and Muntjac deer, and the values between Yeso Sika deer and other species (sheep, cattle, horse, pig, mouse, human and chimpanzee) were 6.63%, 7.30%, 12.55%, 13.03%, 23.59%, 24.82% and 25.04%, respectively. Among them, the highest value of divergence was recognized in ATPase8, and the second structure of ATPase8 showed a difference between the Yeso Sika deer and Muntjac deer as a result of the substitution of 34His→Tyr and 49Thr→Ile. In addition, we identified a substitution of an amino‐acid sequence (19Thr→Ala) between the Yeso Sika deer and Yakushima Sika deer (C. n. yakushimae). From these results, ATPase8 was also a variable region in Cervidae.     

Proteome analysis of cashmere

As an analysis of the cashmere proteins by Type IV 2‐DE, ten kinds of components, including three components with molecular mass 42–50 kDa whose expression level increased in the winter, were separated. In analyzing nine components of these ten using a mass spectrometer, the three components of molecular mass 70–120 kDa and pI 5.3 were identified as keratin type II microfibrillar (accession no. KRSHL2 ), keratin 48 k type I microfibrillar component 8c‐1 (accession no. KRSHL1 ) and cytosolic phospholipase A2 (accession no. O77793 ), respectively. The three components whose expression level increased in the winter, were identified as keratin type I microfibrillar 48 kDa component 8C‐1 (accession no. P02534 ) and keratin type I microfibrillar 47.6 kDa (accession no. P25690 ) (pI 5.2/42 kDa), keratin type II microfibrillar component 7C (accession no. P15241 ) and keratin typeII‐sheep (accession no. S34165 ) (pI 5.5/45 kDa), and the keratin type II microfibrillar component 5 (accession no. P25691 ) (pI 5.8–6.0/45 kDa), respectively. The three components of less than 17 kDa were identified as hair keratin type II intermediate filament (accession no. CAA51836 ) (pI 5.2) and keratin high‐sulfur matrix protein IIIB2 (accession no. P02447 ) with a different isoelectric point (pI 5.4 and 5.9), respectively.