The complete mitochondrial genome of Membranipora villosa Hincks, 1880 (Bryozoa: Gymnolaemata: Cheilostomatida): phylogenetic relationship of two kelp-encrusting bryozoans within the suborder Membraniporina.

The two commonest kelp-encrusting bryozoans, Membranipora villosa and M. membranacea, are difficult to distinguish morphologically. Molecular studies of M. villosa should thus be helpful for the identification of both species because the mitogenome of M. membranacea was already sequenced. The complete mitogenome of M. villosa collected from Sinjido was determined in this study through Illumina NovaSeq sequencing. Maximum-likelihood (ML) analysis was based on concatenated 13 protein-coding genes dataset from nine bryozoan species. The mitogenome length was 15,407 bp, and its gene arrangement was similar to those of the mitogenome of other membraniporids, having 13 PCGs, two ribosomal RNAs, and 22 tRNAs. It had an overall A + T content of 63.7% (29.7% A, 16.7% C, 19.6% G, and 34.0% T). M. villosa and M. membranacea showed sequence differences of 20% for the total length of mitogenome and 16.1.% for 13 PCGs. Molecular data definitely consider them to be separate species. Phylogenetic analyses based on the amino acids of 13 PCGs indicated that M. villosa has the closest relationship with another kelp-encrusting bryozoan, M. membranacea of membraniporids. The phylogenetic position of genera and families within the suborder Membraniporina coincides with the Bayesian phylogenetic analysis of the mixed concatenated alignment consisting of three partitions.

Korean ctenostome bryozoans-observations on living colonies, new records, five new species, and an updated checklist.

This paper describes 12 species of ctenostomes from the marine waters of the Korean Peninsula, including five new species-Alcyonidium bullitum n. sp., Alcyonidium pulposum n. sp., Alcyonidium busanensis n. sp., Immergentia cheongpodensis n. sp. and Penetrantia taeanata n. sp., the latter two constituting shell-borers that ramify within dead mollusk shells. Three previously described species are also newly added to the Korean fauna-Amathia acervata Lamouroux, 1824, Amathia medullaris Mawatari, 1972 and Walkeria prorepens Kubanin, 1992. The nomenclature of known species is updated and a revised checklist of all Korean Ctenostomata is included. New biological information is provided based on observation and microphotography of living and preserved colonies, SEM images of dry material and resin casts of ctenostome borings in mollusk shells.

Regulation of ACS protein stability by cytokinin and brassinosteroid.

A major question in plant biology is how phytohormone pathways interact. Here, we explore the mechanism by which cytokinins and brassinosteroids affect ethylene biosynthesis. Ethylene biosynthesis is regulated in response to a wide variety of endogenous and exogenous signals, including the levels of other phytohormones. Cytokinins act by increasing the stability of a subset of ACC synthases, which catalyze the generally rate-limiting step in ethylene biosynthesis. The induction of ethylene by cytokinin requires the canonical cytokinin two-component response pathway, including histidine kinases, histidine phosphotransfer proteins and response regulators. The cytokinin-induced myc-ACS5 stabilization occurs rapidly (<60 min), consistent with a primary output of this two-component signaling pathway. We examined the mechanism by which another phytohormone, brassinosteroid, elevates ethylene biosynthesis in etiolated seedlings. Similar to cytokinin, brassinosteroid acts post-transcriptionally by increasing the stability of ACS5 protein, and its effects on ACS5 were additive with those of cytokinin. These data suggest that ACS is regulated by phytohormones through regulatory inputs that probably act together to continuously adjust ethylene biosynthesis in various tissues and in response to various environmental conditions.

Eto Brute? Role of ACS turnover in regulating ethylene biosynthesis.

Ethylene influences many plant growth and developmental processes. To achieve this diversity of function, the biosynthesis of this gaseous hormone is tightly regulated by a diverse array of factors, including developmental cues, wounding, biotic and abiotic stresses, and other phytohormones. Many studies have demonstrated that differential transcription of 1-aminocyclopropane-1-carboxylate synthase (ACS) gene family members is an important factor regulating ethylene production in response to different stimuli. Recently, several studies, focusing primarily on the Arabidopsis eto mutants, have indicated that the regulation of ACS protein stability also plays a significant role in the control of ethylene biosynthesis. Here, we review this post-transcriptional control of ethylene biosynthesis and discuss the mechanisms that underlie it.

The eto1, eto2, and eto3 mutations and cytokinin treatment increase ethylene biosynthesis in Arabidopsis by increasing the stability of ACS protein.

The Arabidopsis ethylene-overproducing mutants eto1, eto2, and eto3 have been suggested to affect the post-transcriptional regulation of 1-aminocyclopropane-1-carboxylic acid synthase (ACS). Here, we present the positional cloning of the gene corresponding to the dominant eto3 mutation and show that the eto3 phenotype is the result of a missense mutation within the C-terminal domain of ACS9, which encodes one isoform of the Arabidopsis ACS gene family. This mutation is analogous to the dominant eto2 mutation that affects the C-terminal domain of the highly similar ACS5. Analysis of purified recombinant ACS5 and epitope-tagged ACS5 in transgenic Arabidopsis revealed that eto2 does not increase the specific activity of the enzyme either in vitro or in vivo; rather, it increases the half-life of the protein. In a similar manner, cytokinin treatment increased the stability of ACS5 by a mechanism that is at least partially independent of the eto2 mutation. The eto1 mutation was found to act by increasing the function of ACS5 by stabilizing this protein. These results suggest that an important mechanism by which ethylene biosynthesis is controlled is the regulation of the stability of ACS, mediated at least in part through the C-terminal domain.