Karl M. Koshlap

Works (3)

Updated: July 5th, 2023 16:02

2003 journal article

Naturally-occurring modification restricts the anticodon domain conformational space of tRNA(Phe)

JOURNAL OF MOLECULAR BIOLOGY, 334(5), 901–918.

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
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)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

2000 journal article

Modified constructs of the tRNA T Psi C domain to probe substrate conformational requirements of m(1)A(58) and m(5)U(54) tRNA methyltransferases

NUCLEIC ACIDS RESEARCH, 28(6), 1374–1380.

By: R. Sengupta n, S. Vainauskas, C. Yarian*, E. Sochacka, A. Malkiewicz, R. Guenther, K. Koshlap*, P. Agris*

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
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)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

1999 journal article

A distinctive RNA fold: The solution structure of an analogue of the yeast tRNA(Phe) T psi C domain

BIOCHEMISTRY, 38(27), 8647–8656.

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
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)
UN Sustainable Development Goal Categories
Source: Web Of Science
Added: August 6, 2018

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