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1.
Photochem Photobiol ; 95(6): 1369-1375, 2019 11.
Article in English | MEDLINE | ID: mdl-31230349

ABSTRACT

The experimental evidence for the growth-promoting mechanism and the efficiency of energy transfer (EET) of LH4 under low light are still not available. To elucidate the light adaption mechanism of LH4, we deleted the genes pucBAd involved in the synthesis of the α/ß polypeptides of LH4 in Rhodopseudomonas palustris CGA009. Compared to wild strain, the growth rate of pucBAd mutant significantly decreased under low light, while there were no significant changes in the growth rate, the contents and compositions of photopigments, absorption spectra of cell lysates under high light. Moreover, the fluorescence quantum efficiency (FQE) was used to further compare the EET between LH2 and LH4. The FQE in LH4 increased up to 1.5-fold than did in LH2. Collectively, this study showed that LH4 could provide more and high energetic state photons for promoting bacterial phototrophic growth in response to low-light environment.


Subject(s)
Light , Photosystem II Protein Complex/physiology , Rhodopseudomonas/physiology , Gene Deletion , Gene Expression Regulation, Bacterial , Pigments, Biological/metabolism , Protein Isoforms
2.
Fish Shellfish Immunol ; 56: 445-449, 2016 Sep.
Article in English | MEDLINE | ID: mdl-27474446

ABSTRACT

The noble scallop Chlamys nobilis has been an important marine cultured bivalve in the Southern Sea of China for decades. However, large-scale mortality events often occurred during the scallop' cultivation. As one of AMPs (antimicrobial peptides), big defensin is an important component of the innate immunity against pathogenic microorganisms in invertebrates. In order to investigate whether the big defensin can play a role in the immune defense against pathogenic microorganisms in noble scallop, a big defensin gene from the hemocytes of Chlamys nobilis (CnBD) was cloned, and the mRNA level was measured after an acute Vibrio parahaemolyticus challenge of 36 h. The CnBD cDNA contains an open reading frame (ORF) of 381 bp encoding a peptide of 126 amino acids residues. The deduce amino acid sequence of CnBD shows a high similarity with that from Argopecten irradians and displays common features of big defensin, indicating that CnBD is a new member of the big defensin family. Compared with the control group, the relative mRNA level of CnBD was significantly up-regulated at 3, 24 and 36 h. The present result indicated that CnBD played an immune role against bacterial infection in noble scallop.


Subject(s)
Defensins/genetics , Immunity, Innate , Pectinidae/genetics , Pectinidae/immunology , Vibrio parahaemolyticus/physiology , Amino Acid Sequence , Animals , Base Sequence , Cloning, Molecular , DNA, Complementary/genetics , DNA, Complementary/metabolism , Defensins/chemistry , Defensins/metabolism , Hemocytes/immunology , Hemocytes/metabolism , Pectinidae/metabolism , Pectinidae/microbiology , Phylogeny , RNA, Messenger/genetics , RNA, Messenger/metabolism , Sequence Alignment , Up-Regulation
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