Results 61 to 70 of about 3,855 (167)

RNA 3'-tail synthesis in Streptomyces: in vitro and in vivo activities of RNase PH, the SCO3896 gene product and polynucleotide phosphorylase.

open access: yesMicrobiology, 2006
As in other bacteria, 3'-tails are added post-transcriptionally to Streptomyces coelicolor RNA. These tails are heteropolymeric, and although there are several candidates, the enzyme responsible for their synthesis has not been definitively identified ...
P. Bralley   +4 more
semanticscholar   +1 more source

Genetic dissection of domestication traits in interspecific chickpea populations

open access: yesThe Plant Genome, Volume 17, Issue 1, March 2024.
Abstract Chickpea (Cicer arietinum) is a pulse crop that provides an integral source of nutrition for human consumption. The close wild relatives Cicer reticulatum and Cicer echinospermum harbor untapped genetic diversity that can be exploited by chickpea breeders to improve domestic varieties.
Toby E. Newman   +7 more
wiley   +1 more source

A nucleotidyltransferase toxin inhibits growth of Mycobacterium tuberculosis through inactivation of tRNA acceptor stems

open access: yesScience Advances, 2020
The human pathogen Mycobacterium tuberculosis produces a toxin that can stall bacterial growth by blocking the activity of tRNAs. Toxin-antitoxin systems are widespread stress-responsive elements, many of whose functions remain largely unknown.
Yiming Cai   +9 more
semanticscholar   +2 more sources

The frontier between cell and organelle: genome analysis of Candidatus Carsonella ruddii [PDF]

open access: yes, 2007
Background Bacterial symbioses are widespread among insects. The early establishment of such symbiotic associations has probably been one of the key factors for the evolutionary success of insects, since it may have allowed access to novel ecological ...
Gil, Rosario   +5 more
core   +4 more sources

Does 3'-terminal poly(A) stabilize human fibroblast interferon mRNA in oocytes of Xenopus laevis?

open access: yesProceedings of the National Academy of Sciences of the United States of America, 1978
Polynucleotide phosphorylase (polyribonucleotide:orthophosphate nucleotidyltransferase, EC 2.7.7.8) purified from Escherichia coli was used enzymatically to deadenylate polyadenylated human fibroblast interferon mRNA preparations obtained from human ...
P. Sehgal, H. Soreq, I. Tamm
semanticscholar   +1 more source

Identification of Genes Potentially Regulated by Human Polynucleotide Phosphorylase (hPNPaseold-35) Using Melanoma as a Model [PDF]

open access: yes, 2013
Human Polynucleotide Phosphorylase (hPNPaseold-35 or PNPT1) is an evolutionarily conserved 3′→5′ exoribonuclease implicated in the regulation of numerous physiological processes including maintenance of mitochondrial homeostasis, mtRNA import and aging ...
Bacolod, Manny D.   +4 more
core   +2 more sources

The influence of the size and nature of basic activators on Clostridium perfringens polynucleotide phosphorylase-catalysed polyadenylic acid synthesis.

open access: yesBiochemical Journal, 1969
1. Basic oligo- and poly-(amino acids) stimulate polyadenylic acid synthesis by purified Clostridium perfringens polynucleotide phosphorylase (nucleoside diphosphate-polyribonucleotide nucleotidyltransferase, EC 2.7.7.8). 2.
P. Fitt, Helga Wille
semanticscholar   +1 more source

A genome-wide structure-based survey of nucleotide binding proteins in M. tuberculosis [PDF]

open access: yes
Nucleoside tri-phosphates (NTP) form an important class of small molecule ligands that participate in, and are essential to a large number of biological processes. Here, we seek to identify the NTP binding proteome (NTPome) in M.
Bhagavat, Raghu   +6 more
core   +1 more source

Absence of functional TolC protein causes increased stress response gene expression in Sinorhizobium meliloti [PDF]

open access: yes, 2010
The TolC protein from Sinorhizobium meliloti has previously been demonstrated to be required for establishing successful biological nitrogen fixation symbiosis with Medicago sativa.
Becker, Jorg D.   +5 more
core   +3 more sources

The preferential loss of the polylysine- or polyornithine-stimulated activity of Clostridium perfringens polynucleotide phosphorylase during proteolysis.

open access: yesBiochemical Journal, 1969
1. An improved method for the purification of Clostridium perfringens polynucleotide phosphorylase (nucleoside diphosphate-polyribonucleotide nucleotidyltransferase, EC 2.7.7.8) is described. The product was stable and was highly stimulated by polylysine
P. Fitt, H. Wille
semanticscholar   +1 more source

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