Eric A. Galburt

article

Conformational selection and induced fit as a useful framework for molecular motor mechanisms

Eric A. Galburt, Eric J. Tomko

Biophysical Chemistry > 2017 > 223 > C > 11-16

The linkage between macromolecular binding and conformational change that is ubiquitous in biological molecules can be understood in the context of the mechanisms of conformational selection and induced fit. Here, we explore mappings between these mechanisms of ligand binding and those underlying the translocation of molecular motors and the nucleic acid unwinding of helicases. The mechanism of biased...

chapter

His-Cys Box Homing Endonucleases

Eric A. Galburt, Melissa S. Jurica

Nucleic Acids and Molecular Biology > Homing Endonucleases and Inteins > 85-102

Homing endonucleases are often grouped into four families based on distinct sequence motifs. One of these families is known as the His-Cys box homing endonucleases and contains two clusters of conserved histidine and cysteine residues over a central 100 amino acid region. At last count, 23 members of this family had been identified. The open reading frames (ORFs) of these proteins are contained within...

article

CarD integrates three functional modules to promote efficient transcription, antibiotic tolerance, and pathogenesis in mycobacteria

Ashley L. Garner, Leslie A. Weiss, Ana Ruiz Manzano, Eric A. Galburt, more

Molecular Microbiology > 93 > 4 > 682 - 697

Although the basic mechanisms of prokaryotic transcription are conserved, it has become evident that some bacteria require additional factors to allow for efficient gene transcription. CarD is an RNA polymerase (RNAP)‐binding protein conserved in numerous bacterial species and essential in mycobacteria. Despite the importance of CarD, its function at transcription complexes remains unclear. We have...

article

RNA polymerase pushing

Eric A. Galburt, Juan M.R. Parrondo, Stephan W. Grill

Biophysical Chemistry > 2011 > 157 > 1-3 > 43-47

Molecular motors can exhibit Brownian ratchet or power stroke mechanisms. These mechanistic categories are related to transition state position: An early transition state suggests that chemical energy is stored and then released during the step (stroke) while a late transition state suggests that the release of chemical energy rectifies thermally activated motion that has already occurred (ratchet)...

article

Single molecule transcription elongation

Eric A. Galburt, Stephan W. Grill, Carlos Bustamante

Methods > 2009 > 48 > 4 > 323-332

Single molecule optical trapping assays have now been applied to a great number of macromolecular systems including DNA, RNA, cargo motors, restriction enzymes, DNA helicases, chromosome remodelers, DNA polymerases and both viral and bacterial RNA polymerases. The advantages of the technique are the ability to observe dynamic, unsynchronized molecular processes, to determine the distributions of experimental...

article

The Origin of Short Transcriptional Pauses

Martin Depken, Eric A. Galburt, Stephan W. Grill

Biophysical Journal > 2009 > 96 > 6 > 2189-2193

RNA polymerases are protein molecular machines that transcribe genetic information from DNA into RNA. The elongation of the RNA molecule is frequently interrupted by pauses, the detailed nature of which remains controversial. Here we ask whether backtracking, the central mechanism behind long pauses, could also be responsible for short pauses normally attributed to the ubiquitous pause state. To this...

article

Catalytic Mechanisms of Restriction and Homing Endonucleases

Eric A. Galburt, Barry L. Stoddard

Biochemistry > 2002 > 41 > 47 > 13851 - 13860

article

Structure of a tRNA Repair Enzyme and Molecular Biology Workhorse - T4 Polynucleotide Kinase

Eric A. Galburt, John Pelletier, Geoffrey Wilson, Barry L. Stoddard

Structure > 2002 > 10 > 9 > 1249-1260

T4 phage polynucleotide kinase (PNK) was identified over 35 years ago and has become a staple reagent for molecular biologists. The enzyme displays 5'-hydroxyl kinase, 3'-phosphatase, and 2',3'-cyclic phosphodiesterase activities against a wide range of substrates. These activities modify the ends of nicked tRNA generated by a bacterial response to infection and facilitate repair by T4 RNA ligase...

article

Conformational Changes and Cleavage by the Homing Endonuclease I-PpoI: A Critical Role for a Leucine Residue in the Active Site

Eric A. Galburt, Meggen S. Chadsey, Melissa S. Jurica, Brett S. Chevalier, more

Journal of Molecular Biology > 2000 > 300 > 4 > 877-887

The homing endonuclease I-PpoI severely bends its DNA target, resulting in significant deformations of the minor and major groove near the scissile phosphate groups. To study the role of conformational changes within the protein catalyst and the DNA substrate, we have determined the structure of the enzyme in the absence of bound DNA, performed gel retardation analyses of DNA binding and bending,...

INFONA - science communication portal

Search results for: Eric A. Galburt

Conformational selection and induced fit as a useful framework for molecular motor mechanisms

His-Cys Box Homing Endonucleases

CarD integrates three functional modules to promote efficient transcription, antibiotic tolerance, and pathogenesis in mycobacteria

RNA polymerase pushing

Single molecule transcription elongation

The Origin of Short Transcriptional Pauses

Catalytic Mechanisms of Restriction and Homing Endonucleases

Structure of a tRNA Repair Enzyme and Molecular Biology Workhorse - T4 Polynucleotide Kinase

Conformational Changes and Cleavage by the Homing Endonuclease I-PpoI: A Critical Role for a Leucine Residue in the Active Site

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