scholarly journals Distamycin-induced inhibition of formation of a nucleoprotein complex between the terminase small subunit G1P and the non-encapsidated end (pacL site) of Bacillus subtilis bacteriophage SPP1

1996 ◽  
Vol 24 (2) ◽  
pp. 282-288 ◽  
Author(s):  
S Chai
Author(s):  
Dwight Anderson ◽  
Charlene Peterson ◽  
Gursaran Notani ◽  
Bernard Reilly

The protein product of cistron 3 of Bacillus subtilis bacteriophage Ø29 is essential for viral DNA synthesis and is covalently bound to the 5’-termini of the Ø29 DNA. When the DNA-protein complex is cleaved with a restriction endonuclease, the protein is bound to the two terminal fragments. The 28,000 dalton protein can be visualized by electron microscopy as a small dot and often is seen only when two ends are in apposition as in multimers or in glutaraldehyde-fixed aggregates. We sought to improve the visibility of these small proteins by use of antibody labeling.


1990 ◽  
Vol 265 (36) ◽  
pp. 22365-22370
Author(s):  
S Bailey ◽  
J Wichitwechkarn ◽  
D Johnson ◽  
B E Reilly ◽  
D L Anderson ◽  
...  

2020 ◽  
Author(s):  
Caillan Crowe-McAuliffe ◽  
Hiraku Takada ◽  
Victoriia Murina ◽  
Christine Polte ◽  
Sergo Kasvandik ◽  
...  

SummaryIn all branches of life, stalled translation intermediates are recognized and processed by ribosome-associated quality-control (RQC) pathways. RQC begins with splitting of stalled ribosomes, leaving an unfinished polypeptide still attached to the large subunit. Ancient and conserved NEMF family RQC proteins target these incomplete proteins for degradation by the addition of C-terminal ‘tails.’ How such tailing can occur without the regular suite of translational components is, however, unclear. Using ex vivo single-particle cryo-EM, we show that C-terminal tailing in Bacillus subtilis is mediated by NEMF protein RqcH in concert with YabO, a protein homologous to, yet distinct from, Hsp15. Our structures reveal how these factors mediate tRNA movement across the ribosomal 50S subunit to synthesize polypeptides in the absence of mRNA or the small subunit.


Viruses ◽  
2018 ◽  
Vol 10 (12) ◽  
pp. 705 ◽  
Author(s):  
Lia M. Godinho ◽  
Mehdi El Sadek Fadel ◽  
Céline Monniot ◽  
Lina Jakutyte ◽  
Isabelle Auzat ◽  
...  

Bacillus subtilis bacteriophage SPP1 is a lytic siphovirus first described 50 years ago [1]. Its complete DNA sequence was reported in 1997 [2]. Here we present an updated annotation of the 44,016 bp SPP1 genome and its correlation to different steps of the viral multiplication process. Five early polycistronic transcriptional units encode phage DNA replication proteins and lysis functions together with less characterized, mostly non-essential, functions. Late transcription drives synthesis of proteins necessary for SPP1 viral particles assembly and for cell lysis, together with a short set of proteins of unknown function. The extensive genetic, biochemical and structural biology studies on the molecular mechanisms of SPP1 DNA replication and phage particle assembly rendered it a model system for tailed phages research. We propose SPP1 as the reference species for a new SPP1-like viruses genus of the Siphoviridae family.


1970 ◽  
Vol 68 (3) ◽  
pp. 277-286 ◽  
Author(s):  
Nobuyoshi SHIMIZU ◽  
Kin-ichiro MIURA ◽  
Hatsuo AOKI

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