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Gold, D.

Publications and source records attributed to Gold, D..

2 recordsLinked to original sources

Low-pH conditions drive transient changes in shell calcification and the microbiome in a pH-resistant strain of the the Pacific oyster Magallana gigas

The study explores the effects of elevated pCO2 on shell calcification, microbiome composition, and gene expression in a strain of Pacific oyster (Magallana gigas) selectively bred for low-pH resistance. Juvenile oysters reared under low-pH conditions exhibited increased shell mass compared to the control population by 51 days post-fertilization, despite high variance in shell size at earlier stages. Microbiome analyses revealed significant shifts in community composition under low-pH conditions, particularly in bacterial taxa involved in CO2 production and biogeochemical cycling, which could influence carbonate chemistry within oyster tissues. Gene expression profiling demonstrates differential regulation of genes related to biomineralization, immunity, and microbial interactions under low-pH conditions. For example, multiple carbonic anhydrases exhibited treatment-specific expression patterns, suggesting a role in adapting to low-pH environments. Observed changes in immune-related genes imply a relaxation of immune responses, potentially reflecting resource reallocation toward calcification processes. These results collectively support the "dysbiosis hypothesis," where oysters adapt to environmental stress by modulating their microbiomes and gene expression. Future studies should investigate whether these responses are consistent across oyster strains and environmental conditions, providing insights into the resilience of aquaculture species to ocean acidification. SUMMARY STATEMENTElevated pCO2 impacts Pacific oyster calcification, microbiome composition, and gene expression, suggesting genetic adaptation and microbiome shifts may be crucial for resilience to ocean acidification.

systems biology↗

A pivot-tether model for nucleosome recognition by the chromosomal passenger complex

Spatial restriction of Aurora B to centromeres during prometaphase and metaphase enables it to phosphorylate proteins necessary for spindle assembly checkpoint signalling and biorientation of chromosomes on the mitotic spindle. Aurora B binding to T3-phosphorylated histone H3 (H3pT3) nucleosomes requires a multivalent targeting module, the chromosomal passenger complex (CPC), consisting of survivin, borealin, and INCENP. To shed light on how these components mediate CPC localisation during prometaphase and metaphase, we determined the structure of the CPC targeting module in complex with haspin-phosphorylated H3pT3-nucleosomes by cryo-electron microscopy. This structure shows how the N-terminus of borealin and the survivin BIR domain act as pivot and flexible tethering points, respectively, to increase CPC affinity for H3pT3 nucleosomes without limiting it to a specific orientation. We demonstrate that this flexible, yet constrained pivot-tether arrangement is important for the control of spindle assembly checkpoint signalling by Aurora B.

cell biology↗