Mangroves stand out as one of the most diverse and biologically significant natural systems in the world. Playing critical roles in maintaining the health and productivity of coastal ecosystems, mangroves provide a range of services and functions, including habitat for local fauna and flora, food and other goods, carbon sequestration, and protection from natural disasters such as storm surges and coastal erosion. It is also evident that mangroves face several threats, which have already led to the gradual depletion of mangrove areas worldwide. Based on the analysis of current and related historical literature and data, this review summarises mangrove functions and the threats and challenges associated with mangrove management practices. Our findings suggest that coastal development, expanded aquaculture, deforestation, climate change, and other associated implications such as eutrophication, diseases, and pollution are the major factors posing threats to mangrove sustainability. We also highlight the various challenges, such as land use conflict, a lack of stringent regulatory actions, inadequate policy and government frameworks, and a lack of community awareness, that underlie ineffective mangrove management. The implementation of inclusive and coordinated approaches involving stakeholders from different backgrounds and interests, governmental and non-governmental organisations, and academia is essential for mangrove restoration and sustainable mangrove management by adapting mitigation strategies.

Modern banana cultivars are primarily interspecific triploid hybrids of two species, Musa acuminata and Musa balbisiana, which respectively contribute the A- and B-genomes. The M. balbisiana genome has been associated with improved vigour and tolerance to biotic and abiotic stresses and is thus a target for Musa breeding programs. However, while a reference M. acuminata genome has recently been released (Nature 488:213–217, 2012), little sequence data is available for the corresponding B-genome.

Type I cytochrome P450 enzyme systems are found in mitochondria and consist of three components, a flavoprotein (adrenodoxin reductase, AdRed), an iron-sulfur protein (adrenodoxin, Adx), and the cytochrome P450; Type II P450 enzymes in the endoplasmic reticulum consist of only two components, P450 reductase and the P450. Genetically engineered fusion proteins of Type II cytochromes P450 (such as steroid 17α- and 21-hydroxylases) produce enzymes with increased activity. To test the consequences of constructing fusions of Type I enzymes, we built fusion proteins based on the cholesterol side-chain cleavage enzyme, P450scc. We constructed expression vectors for three fusion proteins: NH₂-P450scc-AdRed-COOH, P450-AdRed-Adx, and P450scc-Adx-AdRed. The various components were assembled from cassette-like cDNA fragments modified and amplified by polymerase chain reaction (PCR), subcloned into a specially tailored vector, and linked by DNA segments encoding hydrophilic linker peptides. The final vectors were transfected into COS-1 cells, incubated with 22R-hydroxycholesterol, and assayed by the secretion of pregnenolone into the culture medium. Triple transfection of three individual vectors expressing P450scc, AdRed, and Adx yielded more pregnenolone than did transfection with P450scc alone. The P450scc-AdRed and P450scc-Adx-AdRed fusion proteins produced levels of pregnenolone similar to the control triple transfection. However, the P450scc-AdRed-Adx fusion produced substantially more pregnenolone, having an apparent V_max of 9.1 ng of pregnenolone produced per milliliter of medium per 24 hr, compared to a V_max of 1.7 ng/ml per day for the triple transfection. These studies suggest that the association of the various components of the cholesterol side-chain cleavage system is partly responsible for the slow conversion of cholesterol to pregnenolone in vivo, and that adrenodoxin is a key factor in determining the reaction rate. These studies also show that fusion proteins of Type I cytochrome P450 enzymes can be designed to increase enzymatic efficiency.

Studies on codon usage in monocots have focused on grasses, and observed patterns of this taxon were generalized to all monocot species. Here, non-grass monocot species were analysed to investigate the differences between grass and non-grass monocots. First, studies of codon usage in monocots were reviewed. The current information was then extended regarding codon usage, as well as codon-pair context bias, using four completely sequenced non-grass monocot genomes (Musa acuminata, Musa balbisiana, Phoenix dactylifera and Spirodela polyrhiza) for which comparable transcriptome datasets are available. Measurements were taken regarding relative synonymous codon usage, effective number of codons, derived optimal codon and GC content and then the relationships investigated to infer the underlying evolutionary forces. The research identified optimal codons, rare codons and preferred codon-pair context in the non-grass monocot species studied. In contrast to the bimodal distribution of GC₃ (GC content in third codon position) in grasses, non-grass monocots showed a unimodal distribution. Disproportionate use of G and C (and of A and T) in two- and four-codon amino acids detected in the analysis rules out the mutational bias hypothesis as an explanation of genomic variation in GC content. There was found to be a positive relationship between CAI (codon adaptation index; predicts the level of expression of a gene) and GC₃. In addition, a strong correlation was observed between coding and genomic GC content and negative correlation of GC₃ with gene length, indicating a strong impact of GC-biased gene conversion (gBGC) in shaping codon usage and nucleotide composition in non-grass monocots. Optimal codons in these non-grass monocots show a preference for G/C in the third codon position. These results support the concept that codon usage and nucleotide composition in non-grass monocots are mainly driven by gBGC.

Steroidogenesis is initiated by the conversion of cholesterol to pregnenolone by mitochondrial cytochrome P450scc [cholesterol, reduced-adrenal-ferredoxin:oxygen oxidoreductase (side-chain-cleaving); EC 1.14.15.6]. Several subsequent steroidal conversions occur in the endoplasmic reticulum (ER), but the last step in the production of glucocorticoids and mineralocorticoids again occurs in the mitochondria. Although cellular compartmentalization of steroidogenic enzymes appears to be a feature of all steroidogenic pathways, some reports indicate that cholesterol can be converted to pregnenolone outside the mitochondria. To investigate whether P450scc can function outside the mitochondria, we constructed vectors producing P450scc and various fusion enzymes of P450scc with electron-transport proteins and directed their expression to either the ER or the mitochondria. Whether targeted to mitochondria or to the ER, plasmid vectors encoding P450scc and fusion proteins of P450scc with either mitochondrial or microsomal electron-transport proteins produced immunodetectable protein. When expressed in mitochondria, all of these constructions converted 22-hydroxycholesterol to pregnenolone, but when expressed in the ER none of them produced pregnenolone. These results show that P450scc can function only in the mitochondria. Furthermore, it appears to be the mitochondrial environment that is required, rather than the specific mitochondrial electron-transport intermediates.