Biomolecular NMR Assignments最新文献

Backbone resonance assignments of the CPEB3 [101-200] and CPEB3 [294-410].

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-03-29 DOI: 10.1007/s12104-025-10226-5

Harunobu Saito, Yujin Lee, Tomoharu Ueno, Naotaka Sekiyama, Masatomo So, Ayako Furukawa, Kenji Sugase

引用次数: 0

The ¹H, ¹⁵N and ¹³C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1).

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-03-28 DOI: 10.1007/s12104-025-10225-6

Antoine Baudin, Hoang H Dinh, Xiaoping Xu, David S Libich

{"title":"The 1H, 15N and 13C backbone resonance assignments of the N-terminal (1-149) domain of Serpine mRNA Binding Protein 1 (SERBP1).","authors":"Antoine Baudin, Hoang H Dinh, Xiaoping Xu, David S Libich","doi":"10.1007/s12104-025-10225-6","DOIUrl":"https://doi.org/10.1007/s12104-025-10225-6","url":null,"abstract":"Serpine mRNA-Binding Protein 1 (SERBP1) is an RNA-binding protein implicated in diverse cellular functions, including translational regulation, tumor progression, and stress response. It interacts with ribosomal subunits, RNA, and proteins involved in stress granules, contributing to processes such as phase separation and epigenetic regulation. Recent studies have shown SERBP1's role in glioblastoma progression and its involvement in ribosomal regulation. Structurally, SERBP1 contains N- and C-terminal hyaluronan-binding domains, two RG/RGG motifs, and is predicted to be predominantly disordered. Here, we report the backbone resonance assignment and secondary structure propensities of SERBP1's N-terminal residues (1-149). Using NMR spectroscopy, we identified a stable α-helix (residues 28-40) and transient structural elements. These findings provide insight into the structural features of SERBP1 that may mediate its interactions with ribosomal subunits, RNA, and other binding partners, laying a foundation for future structural studies of its functional mechanisms.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2025-03-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143735585","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Correction: Backbone resonance assignment of the catalytic and ATP-binding domain of CpxA from Escherichia coli.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-03-25 DOI: 10.1007/s12104-025-10223-8

Jing Deng, Guofang Zeng, Wenqing Xia, Wei Tang, Zhaofei Chai, Yixiang Liu, Conggang Li, Liqun Huang, Ling Jiang

引用次数: 0

Chemical shift assignments of N-terminal dsRNA binding domains dsRBD1 and dsRBD2 of Arabidopsis thaliana DRB5.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-03-24 DOI: 10.1007/s12104-025-10224-7

Priti Chanda Behera, Sneha Paturi, Mandar V Deshmukh

引用次数: 0

Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-02-12 DOI: 10.1007/s12104-025-10222-9

Chu-Ya Wu, Yi-Zong Lee, I-Chen Hu, Liang-Yuan Chiu, Wei-Cheng Ding, Jing Wang, Shih-Che Sue, Shin-Ichi Tate, Ping-Chiang Lyu

{"title":"Backbone resonance assignments of dopamine N-acetyltransferase in free and cofactor-bound states.","authors":"Chu-Ya Wu, Yi-Zong Lee, I-Chen Hu, Liang-Yuan Chiu, Wei-Cheng Ding, Jing Wang, Shih-Che Sue, Shin-Ichi Tate, Ping-Chiang Lyu","doi":"10.1007/s12104-025-10222-9","DOIUrl":"https://doi.org/10.1007/s12104-025-10222-9","url":null,"abstract":"Dopamine N-acetyltransferase (Dat), belonging to the GCN5-related N-acetyltransferase (GNAT) superfamily, is an arylalkylamine N-acetyltransferase (AANAT) that is involved in insects neurotransmitter inactivation and the development of insect cuticle sclerotization. By using the cofactor acetyl coenzyme A (Ac-CoA) as an acetyl group donor, Dat produces acetyl-dopamine through the reaction with dopamine. Although AANATs share similar structural features with the GNAT family, they have low sequence identities among insect AANATs (~ 40%) and between insect AANATs and vertebrate AANATs (~ 12%). A common noticed feature in GNATs is the Ac-CoA-binding induced conformational change, and this is important for further selection and catalysis of its substrate. In AANATs, the conformational changes help the sequential binding mechanism. Here, we report the 1H, 13C and 15N backbone resonance assignments of the 24 kDa Dat from Drosophila melanogaster in the free and Ac-CoA-bound states, and the chemical shift differences revealed a significant conformational change in the α1 region of Dat. These assignments provide a foundation for further investigations of the catalysis and structural regulation of Dat in solution.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2025-02-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143397713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Backbone resonance assignment of the catalytic and ATP-binding domain of CpxA from Escherichia coli.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-02-07 DOI: 10.1007/s12104-025-10218-5

Jing Deng, Guofang Zeng, Wenqing Xia, Wei Tang, Zhaofei Chai, Yixiang Liu, Conggang Li, Liqun Huang, Ling Jiang

引用次数: 0

Backbone and side‑chain ¹H, ¹³C and ¹⁵N resonance assignments and secondary structure determination of the rhizobial FixJ.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-02-01 DOI: 10.1007/s12104-025-10221-w

Akio Horikawa, Rika Okubo, Naoki Hishikura, Riki Watanabe, Kaori Kurashima-Ito, Pooppadi Maxin Sayeesh, Kohsuke Inomata, Masaki Mishima, Hiroyasu Koteishi, Hitomi Sawai, Yoshitsugu Shiro, Teppei Ikeya, Yutaka Ito

{"title":"Backbone and side‑chain 1H, 13C and 15N resonance assignments and secondary structure determination of the rhizobial FixJ.","authors":"Akio Horikawa, Rika Okubo, Naoki Hishikura, Riki Watanabe, Kaori Kurashima-Ito, Pooppadi Maxin Sayeesh, Kohsuke Inomata, Masaki Mishima, Hiroyasu Koteishi, Hitomi Sawai, Yoshitsugu Shiro, Teppei Ikeya, Yutaka Ito","doi":"10.1007/s12104-025-10221-w","DOIUrl":"https://doi.org/10.1007/s12104-025-10221-w","url":null,"abstract":"The symbiotic nitrogen-fixing bacterium Bradyrhizobium japonicum (B.japonicum) enables high soybean yields with little or no nitrogen fertiliser. A two component regulatory system comprising FixL, a histidine kinase with O2-sensing activity, and FixJ, a response regulator, controls the expression of genes involved in nitrogen fixation, such as fixK and nifA. Only under anaerobic conditions, the monophosphate group is transferred from FixL to the N-terminal receiver domain of FixJ (FixJN), which eventually promote the association of the C-terminal effector domain (FixJC) to the promoter regions of the nitrogen-fixation-related genes. Structural biological analyses carried out so far for rhizobial FixJ molecules have proposed a solution structure for FixJ that differs from the crystal structures, in which the two domains are extended. To understand the FixJ activation caused by phosphorylation of the N-terminal domain, which presumably regulates through the interactions between FixJN and FixJC, here we have performed backbone and sidechain resonance assignments of the unphosphorylated state of B. japonicum FixJ.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2025-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143073384","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

¹H, ¹³C, ¹⁵N and ³¹P chemical shift assignment of the first stem-loop Guanidine-II riboswitch from Escherichia coli.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-02-01 DOI: 10.1007/s12104-025-10217-6

Tatjana Koob, Silas Döpp, Harald Schwalbe

引用次数: 0

¹H, ¹⁵N, ¹³C backbone resonance assignment of human Alkbh7.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-01-29 DOI: 10.1007/s12104-025-10219-4

Baboucarr Faal, Jeffrey A Purslow, Vincenzo Venditti

{"title":"1H, 15N, 13C backbone resonance assignment of human Alkbh7.","authors":"Baboucarr Faal, Jeffrey A Purslow, Vincenzo Venditti","doi":"10.1007/s12104-025-10219-4","DOIUrl":"10.1007/s12104-025-10219-4","url":null,"abstract":"The Alkbh7 protein, a member of the Alkylation B (AlkB) family of dioxygenases, plays a crucial role in epigenetic regulation of cellular metabolism. This paper focuses on the NMR backbone resonance assignment of Alkbh7, a fundamental step in understanding its three-dimensional structure and dynamic behavior at the atomic level. Herein, we report the backbone 1H, 15N, 13C chemical shift assignment of the full-length human Alkbh7. Experiments were acquired at 25 °C by heteronuclear multidimensional NMR spectroscopy. Collectively, 70% of the backbone NH resonances were assigned, with 144 out of a possible 205 residues assigned in the 1H-15N TROSY spectrum. Interestingly, peaks from the active site and the C-terminal end of Alkbh7 are not NMR visible, suggesting that these regions are dynamic on the intermediate exchange regime. Using the program TALOS+, a secondary structure prediction was generated from the assigned backbone resonance that is consistent with the previously reported X-ray structure of the enzyme. The reported assignment will permit investigations of the protein structural dynamics anticipated to provide crucial insight regarding fundamental aspects in the recognition and enzyme regulation processes.","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":" ","pages":""},"PeriodicalIF":0.8,"publicationDate":"2025-01-29","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143062988","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0

Chemical shift assignments of DRB2 domains, a dsRNA binding protein in A. thaliana RNAi pathway.

IF 0.8 4区生物学

Biomolecular NMR Assignments Pub Date : 2025-01-29 DOI: 10.1007/s12104-025-10220-x

Upasana Rai, Debadutta Patra, Mandar V Deshmukh

引用次数: 0