Shyamasri Biswas

Works (3)

Updated: July 5th, 2023 15:49

2012 article

Structurally Conserved Nop56/58 N-terminal Domain Facilitates Archaeal Box C/D Ribonucleoprotein-guided Methyltransferase Activity

Gagnon, K. T., Biswas, S., Zhang, X., Brown, B. A., Wollenzien, P., Mattos, C., & Maxwell, E. S. (2012, April 12). Journal of Biological Chemistry.

By: K. Gagnon n, S. Biswas n, X. Zhang n, B. Brown n, P. Wollenzien n, C. Mattos n, E. Maxwell n

MeSH headings : Archaeal Proteins / chemistry; Archaeal Proteins / genetics; Archaeal Proteins / metabolism; Chromosomal Proteins, Non-Histone / chemistry; Chromosomal Proteins, Non-Histone / genetics; Chromosomal Proteins, Non-Histone / metabolism; Methanococcales / chemistry; Methanococcales / genetics; Methanococcales / metabolism; Methyltransferases / chemistry; Methyltransferases / genetics; Methyltransferases / metabolism; Protein Binding; Protein Structure, Tertiary; Ribonucleoproteins / chemistry; Ribonucleoproteins / genetics; Ribonucleoproteins / metabolism
topics (OpenAlex): RNA modifications and cancer; RNA and protein synthesis mechanisms; Cancer-related gene regulation
TL;DR: The archaeal Nop56/58 NTD exhibits a conserved domain structure whose exceptionally stable interaction with fibrillarin plays a role in both RNP assembly and methyltransferase activity. (via Semantic Scholar)
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Added: August 6, 2018

2011 article

Comparative Analysis of the 15.5kD Box C/D snoRNP Core Protein in the Primitive Eukaryote Giardia lamblia Reveals Unique Structural and Functional Features

Biswas, S., Buhrman, G., Gagnon, K., Mattos, C., Brown, B. A., & Maxwell, E. S. (2011, March 2). Biochemistry.

By: S. Biswas n, G. Buhrman n, K. Gagnon *, C. Mattos n, B. Brown n & E. Maxwell n

MeSH headings : Amino Acid Sequence; Animals; Binding Sites / genetics; Circular Dichroism; Crystallography, X-Ray; Giardia lamblia / metabolism; Humans; Methyltransferases / chemistry; Methyltransferases / metabolism; Models, Molecular; Molecular Sequence Data; Molecular Weight; Phylogeny; Protein Binding; Protein Stability; Protein Structure, Secondary; Protein Structure, Tertiary; Protozoan Proteins / chemistry; Protozoan Proteins / genetics; Protozoan Proteins / metabolism; RNA / genetics; RNA / metabolism; Ribonucleoproteins, Small Nucleolar / chemistry; Ribonucleoproteins, Small Nucleolar / classification; Ribonucleoproteins, Small Nucleolar / metabolism; Sequence Homology, Amino Acid; Temperature
topics (OpenAlex): RNA modifications and cancer; RNA and protein synthesis mechanisms; Cancer-related gene regulation
TL;DR: Comp comparative sequence analysis indicated a distinct evolutionary position between Archaea and Eukarya, and the Giardia 15.5kD protein occupies a unique position in the evolution of this box C/D RNP core protein retaining structural and functional features characteristic of both archaeal L7Ae and higher eukaryotic 15. (via Semantic Scholar)
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Added: August 6, 2018

2009 article

Signature amino acids enable the archaeal L7Ae box C/D RNP core protein to recognize and bind the K-loop RNA motif

Gagnon, K. T., Zhang, X., Qu, G., Biswas, S., Suryadi, J., Brown, B. A., & Maxwell, E. S. (2009, November 19). RNA.

By: K. Gagnon n, X. Zhang n, G. Qu n, S. Biswas n, J. Suryadi *, B. Brown n, E. Maxwell n

author keywords: box C/D snoRNA; snoRNP; kink-turn; L7Ae/L30 proteins; RNA-protein interaction
MeSH headings : Amino Acid Motifs / physiology; Amino Acid Sequence; Archaea / genetics; Archaea / metabolism; Archaeal Proteins / chemistry; Archaeal Proteins / genetics; Archaeal Proteins / metabolism; Base Sequence; Binding Sites / genetics; Conserved Sequence; Models, Biological; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; Nucleic Acid Conformation; Protein Binding / genetics; RNA, Archaeal / chemistry; RNA, Archaeal / metabolism; Ribonucleoproteins / chemistry; Ribonucleoproteins / genetics; Ribonucleoproteins / metabolism; Sequence Homology, Amino Acid
topics (OpenAlex): RNA and protein synthesis mechanisms; RNA modifications and cancer; RNA Research and Splicing
TL;DR: These five signature amino acids are distinct for each of the L7Ae/L30 family members, suggesting an evolutionary continuum of these RNA-binding proteins for recognition of the various K-turn motifs contained in their cognate RNAs. (via Semantic Scholar)
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