Karl M. Koshlap

Works (3)

Updated: July 5th, 2023 16:02

2003 article

Naturally-occurring Modification Restricts the Anticodon Domain Conformational Space of tRNA Phe

Stuart, J. W., Koshlap, K. M., Guenther, R., & Agris, P. F. (2003, December 1). Journal of Molecular Biology.

By: J. Stuart n, K. Koshlap n, R. Guenther n & P. Agris n

author keywords: methylation; anticodon dynamics; tRNA position 37; codon recognition; frameshifting
MeSH headings : Anticodon; Base Sequence; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular; Nucleic Acid Conformation; RNA, Transfer, Phe / chemistry
topics (OpenAlex): RNA modifications and cancer; RNA and protein synthesis mechanisms; RNA Research and Splicing
TL;DR: A comparison of the resulting structures indicates that modification of position 37 affects the accuracy of decoding and the maintenance of the mRNA reading frame by restricting anticodon loop conformational space. (via Semantic Scholar)
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Added: August 6, 2018

2000 article

Modified constructs of the tRNA TPsiC domain to probe substrate conformational requirements of m1A58 and m5U54 tRNA methyltransferases

Sengupta, R. (2000, March 15). Nucleic Acids Research.

By: R. Sengupta  n

MeSH headings : Animals; Escherichia coli / enzymology; Kinetics; Magnetic Resonance Spectroscopy; Methylation; Nucleic Acid Conformation; Nucleosides / chemistry; Nucleosides / genetics; Nucleosides / metabolism; RNA Stability; RNA, Transfer, Phe / chemical synthesis; RNA, Transfer, Phe / chemistry; RNA, Transfer, Phe / genetics; RNA, Transfer, Phe / metabolism; Substrate Specificity; Temperature; Tetrahymena pyriformis / enzymology; Thermodynamics; Yeasts / genetics; tRNA Methyltransferases / metabolism
topics (OpenAlex): RNA modifications and cancer; RNA and protein synthesis mechanisms; Genomics and Phylogenetic Studies
TL;DR: It is reported that RAMT can recognize and methylate a TSL heptadecamer, and local conformation around U(54) was found to be an important determinant for the activities of both RAMT and RUMT. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

1999 article

A Distinctive RNA Fold:  The Solution Structure of an Analogue of the Yeast tRNAPhe TΨC Domain,

Koshlap, K. M., Guenther, R., Sochacka, E., Malkiewicz, A., & Agris, P. F. (1999, June 16). Biochemistry.

By: K. Koshlap n, R. Guenther n, E. Sochacka  n, A. Malkiewicz n & P. Agris n

MeSH headings : Anticodon / chemistry; Base Sequence; Crystallography, X-Ray; Models, Molecular; Molecular Sequence Data; Nuclear Magnetic Resonance, Biomolecular / methods; Nucleic Acid Conformation; Pseudouridine / chemistry; RNA, Fungal / chemistry; RNA, Transfer, Phe / chemistry; Saccharomyces cerevisiae / chemistry; Solutions; Uridine / analogs & derivatives; Uridine / chemistry
topics (OpenAlex): RNA modifications and cancer; RNA and protein synthesis mechanisms; Genomics and Phylogenetic Studies
TL;DR: It is believed that the structure determined may represent an intermediate in the folding pathway during the maturation of tRNA, which has a considerable resemblance to the analogous domain in the crystal structure of the full-length yeast tRNAPhe. (via Semantic Scholar)
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Source: Web Of Science
Added: August 6, 2018

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