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Mainstream partial-denitrification with anammox (PD-anammox) process faced the challenge of complex organics involved in real sewage. Herein, PD-anammox coupled with in-situ fermentation was successfully achieved in a full biofilm system formed by three-stage anoxic/oxic reactor to treat real wastewater with low COD/N of 3.6. The total nitrogen (TN) removal efficiency was enhanced to 78.4% ± 3.6% with average TN and ammonium concentrations in effluent of 10.6 and 0.5 mg N/L, respectively. Batch tests confirmed that partial-denitrification was the major nitrite provider for anammox in the anoxic biofilm, while in-situ fermentation could decompose the complex organics to readily-biodegradable organics for full- or partial-denitrification. Additionally, a significant anammox bacteria (Candidatus Brocadia) population was detected in the second (3.53%) and third (4.46%) anoxic zones, while denitrifiers and fermentative bacteria were mainly enriched in the first anoxic zone. This study presents a feasible approach for PD-anammox process in practical application under mainstream condition.

α-Synuclein is a major component of Lewy bodies in Parkinson's disease. Although no signal sequence is apparent, α-synuclein expressed in Escherichia coli is mostly located in the periplasm. The possibilities that α-synuclein translocated into the periplasm across the inner membrane by the SecA or the Tat targeting route identified in bacteria and that α-synuclein was released through MscL were excluded. The signal recognition particle-dependent pathway is involved in the translocation of α-synuclein. The C-terminal 99-to-140 portion of the α-synuclein molecule plays a signal-like role for its translocation into the periplasm, cooperating with the central 61-to-95 section. The N-terminal 1-to-60 region is not required for this translocation.

CheA-short interacts with CheZ to localize CheZ to cell poles. The fifth helical region (residues 112 to 133) from the phosphotransfer domain of CheA interacts with CheZ and becomes ordered and helical, although it lacks a stable fold in the CheA fragment comprising residues 98 to 150 alone. One CheA molecule binds to one CheZ dimer.

alpha-Synuclein (AS) is a main component of Lewy bodies in midbrain dopamine neurons pathologically characteristic of Parkinson's disease. We show that heat shock protein (Hsp) 70 inhibits AS fibril formation via preventing the formation of prefibrillar AS (PreAS), binding with PreAS to impede nuclei formation, and binding with nuclei to retard fibril elongation. Also, Hsp70 suppresses the PreAS-induced permeabilization of vesicular membrane through interactions with PreAS. The substrate-binding domain alone is sufficient for Hsp70 to inhibit AS fibril formation. The binding of Hsp70 with PreAS only requires the substrate-binding subdomain, and the binding with AS nuclei requires the C-terminal lid subdomain as well. The results may form the molecular basis for elucidating the mechanism of AS fibril formation and the crucial roles of chaperones in protecting proteins from toxic conversion in many conformational diseases.