Biomolecular NMR Assignments最新文献_第8页

Backbone resonance assignments of the C-terminal region of human translation initiation factor eIF4B 人翻译起始因子eIF4B c端区域的主链共振分配。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-06-27 DOI: 10.1007/s12104-023-10141-7

Somnath Mondal, Sabrina Rousseau, Vincent Talenton, Cheikh Ahmadou Bamba Thiam, Mikayel Aznauryan, Cameron D. Mackereth

引用次数: 0

NMR resonance assignments of 18.5 kDa complex of Arabidopsis thaliana DRB7.2:DRB4 interaction domains 拟南芥DRB7.2:DRB4相互作用结构域18.5kDa复合物的NMR共振归属。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-31 DOI: 10.1007/s12104-023-10137-3

Sneha Paturi, Mandar V. Deshmukh

引用次数: 0

1H, 13C and 15N backbone and sidechain assignment of the Burkholderia mallei acyl carrier protein 槌状伯克霍尔德菌酰基载体蛋白的1H、13C和15N主链和侧链分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-26 DOI: 10.1007/s12104-023-10136-4

Srdan Matosin, Patrick D. Fischer, Maxim A. Droemer, Eric Baggs, Abu Sayeed Chowdhury, Isidoro Tavares, Scott B. Ficarro, Lisa Rose Warner, Haribabu Arthanari, Rajesh Nagarajan

引用次数: 0

Complete non-proline backbone resonance assignments of the S. aureus neutrophil serine protease inhibitor, EapH1 金黄色葡萄球菌中性粒细胞丝氨酸蛋白酶抑制剂EapH1的完全非脯氨酸骨干共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-10 DOI: 10.1007/s12104-023-10131-9

Nitin Mishra, Indrani Pal, Alvaro I. Herrera, Abhinav Dubey, Haribabu Arthanari, Brian V. Geisbrecht, Om Prakash

引用次数: 1

Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa 铜绿假单胞菌形成功能性淀粉样蛋白FapC的生物膜全长和纤原前单体形式的溶液态核磁共振分配和二级结构倾向。

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-10 DOI: 10.1007/s12104-023-10135-5

Chang-Hyeock Byeon, Pang C. Wang, In-Ja L. Byeon, Ümit Akbey

{"title":"Solution-state NMR assignment and secondary structure propensity of the full length and minimalistic-truncated prefibrillar monomeric form of biofilm forming functional amyloid FapC from Pseudomonas aeruginosa","authors":"Chang-Hyeock Byeon, Pang C. Wang, In-Ja L. Byeon, Ümit Akbey","doi":"10.1007/s12104-023-10135-5","DOIUrl":"10.1007/s12104-023-10135-5","url":null,"abstract":"<div>Functional bacterial amyloids provide structural scaffolding to bacterial biofilms. In contrast to the pathological amyloids, they have a role in vivo and are tightly regulated. Their presence is essential to the integrity of the bacterial communities surviving in biofilms and may cause serious health complications. Targeting amyloids in biofilms could be a novel approach to prevent chronic infections. However, structural information is very scarce on them in both soluble monomeric and insoluble fibrillar forms, hindering our molecular understanding and strategies to fight biofilm related diseases. Here, we present solution-state NMR assignment of 250 amino acid long biofilm-forming functional-amyloid FapC from Pseudomonas aeruginosa. We studied full-length (FL) and shorter minimalistic-truncated (L2R3C) FapC constructs without the signal-sequence that is required for secretion. 91% and 100% backbone NH resonance assignments for FL and L2R3C constructs, respectively, indicate that soluble monomeric FapC is predominantly disordered, with sizeable secondary structural propensities mostly as PP2 helices, but also as α-helices and β-sheets highlighting hotspots for fibrillation initiation interface. A shorter construct showing almost identical NMR chemical shifts highlights the promise of utilizing it for more demanding solid-state NMR studies that require methods to alleviate signal redundancy due to almost identical repeat units. This study provides key NMR resonance assignments for future structural studies of soluble, pre-fibrillar and fibrillar forms of FapC.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 2","pages":"159 - 165"},"PeriodicalIF":0.9,"publicationDate":"2023-05-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9440635","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: 4

Solution NMR backbone assignment of the SASH1 SLy proteins associated disordered region (SPIDER) SASH1 SLy蛋白相关紊乱区(SPIDER)的溶液核磁共振骨架分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-08 DOI: 10.1007/s12104-023-10134-6

Christopher M. Clements, Beat Vögeli, Yiqun G. Shellman, Morkos A. Henen

{"title":"Solution NMR backbone assignment of the SASH1 SLy proteins associated disordered region (SPIDER)","authors":"Christopher M. Clements, Beat Vögeli, Yiqun G. Shellman, Morkos A. Henen","doi":"10.1007/s12104-023-10134-6","DOIUrl":"10.1007/s12104-023-10134-6","url":null,"abstract":"<div>SASH1 is a scaffold protein with context-dependent biological functions in cell adhesion, tumor metastasis, lung development, and pigmentation. As a member of the SLy protein family, it contains the conserved SLY, SH3, and SAM domains. The 19 kDa SLY domain harbors over 70% of the SASH1 variants associated with pigmentation disorders. However, its solution structure or dynamics have not been investigated yet, and its exact position in the sequence is not clearly defined. Based on the bioinformatic and experimental evidence, we propose renaming this region to the SLy Proteins Associated Disordered Region (SPIDER) and defining the exact position to be amino acids 400–554 of SASH1. We have previously identified a variant in this region linked to a pigmentation disorder, S519N. Here, we used a novel deuteration technique, a suite of TROSY-based 3D NMR experiments, and a high-quality HNN to obtain near complete solution backbone assignment of SASH1’s SPIDER. A comparison with the chemical shifts of non-variant (S519) SPIDER shows that the S519N substitution does not alter the free form solution structural propensities of SPIDER. This assignment is the first step to characterize the role of SPIDER in SASH1-mediated cellular functions and provides a model for the future study of sister SPIDER domains in the SLy protein family.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"151 - 157"},"PeriodicalIF":0.9,"publicationDate":"2023-05-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-023-10134-6.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4356446","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 2

1 H, 15 N, and 13 C backbone and side chain resonance assignments of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2 拟南芥甘氨酸富蛋白AtGRP2冷激域的1 H、15 N和13 C主链和侧链共振分配

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-05 DOI: 10.1007/s12104-023-10133-7

Karina C. Pougy, Gilberto Sachetto-Martins, Fabio C. L. Almeida, Anderson S. Pinheiro

{"title":"1 H, 15 N, and 13 C backbone and side chain resonance assignments of the cold shock domain of the Arabidopsis thaliana glycine-rich protein AtGRP2","authors":"Karina C. Pougy, Gilberto Sachetto-Martins, Fabio C. L. Almeida, Anderson S. Pinheiro","doi":"10.1007/s12104-023-10133-7","DOIUrl":"10.1007/s12104-023-10133-7","url":null,"abstract":"<div>AtGRP2 (Arabidopsis thaliana glycine-rich protein 2) is a 19-kDa RNA-binding glycine-rich protein that regulates key processes in A. thaliana. AtGRP2 is a nucleo-cytoplasmic protein with preferential expression in developing tissues, such as meristems, carpels, anthers, and embryos. AtGRP2 knockdown leads to an early flowering phenotype. In addition, AtGRP2-silenced plants exhibit a reduced number of stamens and abnormal development of embryos and seeds, suggesting its involvement in plant development. AtGRP2 expression is highly induced by cold and abiotic stresses, such as high salinity. Moreover, AtGRP2 promotes double-stranded DNA/RNA denaturation, indicating its role as an RNA chaperone during cold acclimation. AtGRP2 is composed of an N-terminal cold shock domain (CSD) followed by a C-terminal flexible region containing two CCHC-type zinc fingers interspersed with glycine-rich sequences. Despite its functional relevance in flowering time regulation and cold adaptation, the molecular mechanisms employed by AtGRP2 are largely unknown. To date, there is no structural information regarding AtGRP2 in the literature. Here, we report the 1H, 15N, and 13C backbone and side chain resonance assignments, as well as the chemical shift-derived secondary structure propensities, of the N-terminal cold shock domain of AtGRP2, encompassing residues 1–90. These data provide a framework for AtGRP2-CSD three-dimensional structure, dynamics, and RNA binding specificity investigation, which will shed light on its mechanism of action.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"143 - 149"},"PeriodicalIF":0.9,"publicationDate":"2023-05-05","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4222548","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 and ILV side-chain methyl NMR resonance assignments of human Rev7/Rev3-RBM1 and Rev7/Rev3-RBM2 complexes 人Rev7/Rev3-RBM1和Rev7/Rev3-RBM2配合物的主链和侧链甲基核磁共振配位

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-02 DOI: 10.1007/s12104-023-10128-4

Gianluca A. Arianna, Dane H. Geddes-Buehre, Dmitry M. Korzhnev

引用次数: 0

Chemical shift assignments of retinal guanylyl cyclase activating protein 5 (GCAP5) with a mutation (R22A) that abolishes dimerization and enhances cyclase activation 具有突变(R22A)的视网膜胍基环化酶激活蛋白5 (GCAP5)的化学移位分配，该突变消除了二聚化并增强了环化酶的激活

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-02 DOI: 10.1007/s12104-023-10129-3

Diana Cudia, Effibe O. Ahoulou, James B. Ames

引用次数: 0

1H, 13C, 15N backbone chemical shift assignments of the extended ARID domain in human AT-rich interactive domain protein 5a (Arid5a) 人类富含at的相互作用结构域蛋白5a (Arid5a)扩展的ARID结构域的1H, 13C, 15N主链化学位移定位

IF 0.9 4区生物学

Biomolecular NMR Assignments Pub Date : 2023-05-02 DOI: 10.1007/s12104-023-10130-w

Julian von Ehr, Sophie Marianne Korn, Lena Weiß, Andreas Schlundt

{"title":"1H, 13C, 15N backbone chemical shift assignments of the extended ARID domain in human AT-rich interactive domain protein 5a (Arid5a)","authors":"Julian von Ehr, Sophie Marianne Korn, Lena Weiß, Andreas Schlundt","doi":"10.1007/s12104-023-10130-w","DOIUrl":"10.1007/s12104-023-10130-w","url":null,"abstract":"<div>The family of AT-rich interactive domain (ARID) containing proteins -Arids- contains 15 members that have almost exclusively been described as DNA-binding proteins. Interestingly, a decade ago the family member Arid5a was found to bind and stabilize mRNAs of immune system key players and thereby account for driving inflammatory and autoimmune diseases. How exactly binding to DNA and RNA is coordinated by the Arid5a ARID domain remains unknown, mainly due to the lack of atom-resolved information on nucleic acid-binding. This in particular applies to the protein’s ARID domain, despite the comfortable size of its core unit for NMR-based investigations. Furthermore, the core domain of ARID domains is found to be extended by functionally relevant, often flexible stretches, but whether such elongations are present and crucial for the versatile Arid5a functions is unknown. We here provide a near-complete NMR backbone resonance assignment of the Arid5a ARID domain with N- and C-terminal extensions, which serves as a basis for further studies of its nucleic acid-binding preferences and targeted inhibition by means of NMR. Our data thus significantly contribute to unravelling mechanisms of Arid5a-mediated gene regulation and diseases.</div>","PeriodicalId":492,"journal":{"name":"Biomolecular NMR Assignments","volume":"17 1","pages":"121 - 127"},"PeriodicalIF":0.9,"publicationDate":"2023-05-02","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://link.springer.com/content/pdf/10.1007/s12104-023-10130-w.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"4440021","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

引用次数: 0