Jindong Zhao

Co-authors

Following

Followers

Research Focus & Metrics

Explore full metrics on Scilit

Academic Career Length

29Years (1998-Present)

(Calculated once Scilit publication data is synced: current year − year of first publication + 1)

Representative Publications

View All Publications

29 March 2004 in Proceedings of the National Academy of Sciences

Journal Article

HetR homodimer is a DNA-binding protein required for heterocyst differentiation, and the DNA-binding activity is inhibited by PatS

Xu Huang

Yuqing Dong

Jindong Zhao

HetR plays a key role in regulation of heterocyst differentiation. When the Cys-48 residue of the HetR from Anabaena sp. PCC 7120 was replaced with an Ala residue, the mutant HetR (HetR _C48A ) could not dimerize, indicating that HetR forms a homodimer through a disulfide bond. The Anabaena strain C48, containing the hetRc48a gene, could not produce HetR homodimer and failed to form heterocyst. We show that HetR is a DNA-binding protein and that its homodimerization is required for the DNA binding. HetR binds the promoter regions of hetR , hepA , and patS , suggesting a direct control of the expression of these genes by HetR. We present evidence that shows that the up-regulation of patS and hetR depends on DNA binding by HetR dimer. The pentapeptide RGSGR, which is present at the C terminus of PatS and blocks heterocyst formation, inhibits the DNA binding of HetR and prevents hetR up-regulation.

22 May 2015 in Cell Research

Journal Article

Structural organization of an intact phycobilisome and its association with photosystem II

Leifu Chang

Xianwei Liu

Yanbing Li

Cui-Cui Liu

Fan Yang

Sen-Fang Sui

Phycobilisomes (PBSs) are light-harvesting antennae that transfer energy to photosynthetic reaction centers in cyanobacteria and red algae. PBSs are supermolecular complexes composed of phycobiliproteins (PBPs) that bear chromophores for energy absorption and linker proteins. Although the structures of some individual components have been determined using crystallography, the three-dimensional structure of an entire PBS complex, which is critical for understanding the energy transfer mechanism, remains unknown. Here, we report the structures of an intact PBS and a PBS in complex with photosystem II (PSII) from Anabaena sp. strain PCC 7120 using single-particle electron microscopy in combination with biochemical and molecular analyses. In the PBS structure, all PBP trimers and the conserved linker protein domains were unambiguously located, and the global distribution of all chromophores was determined. We provide evidence that ApcE and ApcF are critical for the formation of a protrusion at the bottom of PBS, which plays an important role in mediating PBS interaction with PSII. Our results provide insights into the molecular architecture of an intact PBS at different assembly levels and provide the basis for understanding how the light energy absorbed by PBS is transferred to PSII.

17 September 2021 in Nature Communications

Journal Article

Structural insight into the mechanism of energy transfer in cyanobacterial phycobilisomes

Lvqin Zheng

Zhenggao Zheng

Xiying Li

Guopeng Wang

Kun Zhang

Ning Gao

Phycobilisomes (PBS) are the major light-harvesting machineries for photosynthesis in cyanobacteria and red algae and they have a hierarchical structure of a core and peripheral rods, with both consisting of phycobiliproteins and linker proteins. Here we report the cryo-EM structures of PBS from two cyanobacterial species, Anabaena 7120 and Synechococcus 7002. Both PBS are hemidiscoidal in shape and share a common triangular core structure. While the Anabaena PBS has two additional hexamers in the core linked by the 4th linker domain of ApcE (L_CM). The PBS structures predict that, compared with the PBS from red algae, the cyanobacterial PBS could have more direct routes for energy transfer to ApcD. Structure-based systematic mutagenesis analysis of the chromophore environment of ApcD and ApcF subunits reveals that aromatic residues are critical to excitation energy transfer (EET). The structures also suggest that the linker protein could actively participate in the process of EET in both rods and the cores. These results provide insights into the organization of chromophores and the mechanisms of EET within cyanobacterial PBS.

22 January 2007 in Molecular Microbiology

Journal Article

MreB is important for cell shape but not for chromosome segregation of the filamentous cyanobacterium Anabaena sp. PCC 7120

Bin Hu

Guohua Yang

Weixing Zhao

Yingjiao Zhang

Jindong Zhao

11 February 2022 in Science Advances

Journal Article

Environmental DNA captures native and non-native fish community variations across the lentic and lotic systems of a megacity

Yitao Zheng

Chunxia Dong

Globally, urbanization poses a major threat to terrestrial biodiversity, yet its impact on fish diversity is poorly understood, mainly because of surveying difficulties. In this study, environmental DNA metabarcoding was used to survey fish communities at 109 lentic and lotic sites across Beijing, and how environmental variables affect fish biodiversity at fine urban spatial scales was investigated. We identified 52 native and 23 non-native taxa, with lentic and lotic waters harboring both common and habitat-specific species. Water quality strongly affected native fish diversity, especially in lentic systems, but had little influence on non-native diversity. Fish diversity showed little response to urban land cover variation, but the relative sequence abundance of non-natives in lotic waters increased linearly with distance from the city center. Our findings illustrate the complex effects of urbanization on native versus non-native fishes in different aquatic habitats and highlight the distinctive considerations needed to conserve urban aquatic biodiversity.

28 April 1998 in Proceedings of the National Academy of Sciences

Journal Article

Evidence that HetR protein is an unusual serine-type protease

Ruanbao Zhou

Xingcheng Wei

Nan Jiang

Huiguang Li

Yuqing Dong

Jindong Zhao

The hetR gene plays a very important role in cell differentiation of heterocystous cyanobacteria. To understand the mechanism of the hetR gene product in regulation of heterocyst differentiation, the recombinant HetR protein (rHetR) was overproduced in Escherichia coli . Purified rHetR was unstable and degraded easily in solution. Phenylmethanesulfonyl fluoride, a serine-type protease inhibitor, prevented the degradation and was shown to modify covalently rHetR. Dansyl fluoride (DnsF), another serine-type protease inhibitor, also covalently modifies rHetR as shown by electrophoresis and electroblotting of the labeled rHetR and by MS. The labeling of rHetR with phenylmethanesulfonyl fluoride and DnsF was at the same site of rHetR and required Ca ²⁺ . S179N-rHetR, a mutant protein from strain 216 of Anabaena PCC 7120, which cannot differentiate heterocysts because of the mutation, was also overproduced and characterized. Although S170N-rHetR still can be labeled with DnsF, no proteolysis was observed, suggesting that Ser179 is involved in proteolytic activity. DnsF-labeled rHetR was digested with trypsin, and the labeled peptide was isolated and sequenced. The labeled peptide matches a sequence from HetR. These results show that HetR is a protease.

About Me

Dr. Zhao obtained his B. Sci. degree in biology from Southwest University, China. He was admitted to the graduate school of Chinese Academy of Sciences (CAS) for studying the ecology of algae. He received a fellowship from CAS and studied in University of Texas at Austin in the field of cyanobacterial photosynthesis as a graduate student. He completed his Ph.D. in Plant Physiology in 1990. Dr. Zhao then went to Penn State University as a postdoctoral scholar and continued studying the photosynthetic electron transfer of cyanobacteria. After his postdoctoral research, Dr. Zhao briefly joined Applied Biosystems in California as a research scientist before he returned to China and became an associated professor in Peking University in 1994. He was promoted to professor in 1998. From 2007 to 2018, Dr. Zhao served as director in Institute of Hydrobiology, CAS, which was established in 1930. Dr. Zhao was elected a member of CAS in 2007 and a member of TWAS in 2010. Dr. Zhao’s lab focuses on two aspects of cyanobacteria, the mechanisms of multicellularity and photosynthesis. The former includes heterocyst differentiation, cell-to-cell connections and communications, and the latter includes light harvesting of phycobilisomes and photosynthetic electron transfer. His group is also interested in study of freshwater cyanobacterial blooms.

Jindong Zhao

Jindong Zhao

Research Focus & Metrics

Academic Career Length

Publication Type Breakdown

Representative Publications

About Me