scholarly journals A La protein requirement for efficient pre-tRNA folding

2003 ◽  
Vol 22 (24) ◽  
pp. 6562-6572 ◽  
Author(s):  
G. Chakshusmathi
2009 ◽  
Vol 33 (4) ◽  
pp. 674-681 ◽  
Author(s):  
Xiao-Zhi LIN ◽  
Xiao-Jun XIE ◽  
Yi-Ping LUO

1980 ◽  
Vol 3 (1) ◽  
pp. 11-14 ◽  
Author(s):  
C. Giordano ◽  
N.G. De Santo ◽  
M. Pluvio ◽  
V.A. Di Leo ◽  
G. Capodicasa ◽  
...  

This work was presented in part at the 12th Annual Contractor's Conference of the National Institutes of Arthritis, Metabolism and Digestive Diseases, Bethesda, USA, January 15, 1979 and the Congress of the International Society for Artificial Internal Organs at the symposium on CAPD, New York Hilton, New York, April 19, 1979.


2019 ◽  
Vol 116 (46) ◽  
pp. 23075-23082
Author(s):  
Kathleen A. Leamy ◽  
Ryota Yamagami ◽  
Neela H. Yennawar ◽  
Philip C. Bevilacqua

RNA folding is often studied by renaturing full-length RNA in vitro and tracking folding transitions. However, the intracellular transcript folds as it emerges from the RNA polymerase. Here, we investigate the folding pathways and stability of numerous late-transcriptional intermediates of yeast and Escherichia coli transfer RNAs (tRNAs). Transfer RNA is a highly regulated functional RNA that undergoes multiple steps of posttranscriptional processing and is found in very different lengths during its lifetime in the cell. The precursor transcript is extended on both the 5′ and 3′ ends of the cloverleaf core, and these extensions get trimmed before addition of the 3′-CCA and aminoacylation. We studied the thermodynamics and structures of the precursor tRNA and of late-transcriptional intermediates of the cloverleaf structure. We examined RNA folding at both the secondary and tertiary structural levels using multiple biochemical and biophysical approaches. Our findings suggest that perhaps nature has selected for a single-base addition to control folding to the functional 3D structure. In near-cellular conditions, yeast tRNAPhe and E. coli tRNAAla transcripts fold in a single, cooperative transition only when nearly all of the nucleotides in the cloverleaf are transcribed by indirectly enhancing folding cooperativity. Furthermore, native extensions on the 5′ and 3′ ends do not interfere with cooperative core folding. This highly controlled cooperative folding has implications for recognition of tRNA by processing and modification enzymes and quality control of tRNA in cells.


1997 ◽  
Vol 77 (2) ◽  
pp. 197-212 ◽  
Author(s):  
Jens Kondrup ◽  
Klaus Nielsen ◽  
Anders Juul

Patients with cirrhosis of the liver require an increased amount of protein to achieve N balance. However, the utilization of protein with increased protein intake, i.e. the slope from regression analysis of N balance v. intake, is highly efficient (Nielsen et al. 1995). In the present study, protein requirement and protein utilization were investigated further by measuring protein synthesis and degradation. In two separate studies, five or six patients with cirrhosis of the liver were refed on a balanced diet for an average of 2 or 4 weeks. Protein and energy intakes were doubled in both studies. Initial and final whole-body protein metabolism was measured in the fed state by primed continous [15N]glycine infusion. Refeeding caused a statistically significant increase of about 30% in protein synthesis in both studies while protein degradation was only slightly affected. The increase in protein synthesis was associated with significant increases in plasma concentrations of total amino acids (25%), leucine (58%), isoleucine (82%), valine (72%), proline (48%) and triiodothyronine (27%) while insulin, growth hormone, insulin-like growth factor (IGF)-I and IGF-binding protein-3 were not changed significantly. The results indicate that the efficient protein utilization is due to increased protein synthesis, rather than decreased protein degradation, and suggest that increases in plasma amino acids may be responsible for the increased protein synthesis. A comparison of the patients who had a normal protein requirement with the patients who had an increased protein requirement suggests that the increased protein requirement is due to a primary increase in protein degradation. It is speculated that this is due to low levels of IGF-I secondary to impaired liver function, since initial plasma concentration of IGF-I was about 25% of control values and remained low during refeeding.


1954 ◽  
Vol 44 (3) ◽  
pp. 270-273 ◽  
Author(s):  
E. F. Annison ◽  
Margaret I. Chalmers ◽  
S. B. M. Marshall ◽  
R. L. M. Synge

1. Ruminal ammonia concentrations were measured in sheep receiving basal diets of hay and meals with various supplementary sources of protein. Ammonia production from groundnut meal was great and from maize products slight. Herring meal behaved in an intermediate way.2. The extent of ammonia production from a given amount of protein-rich material was decreased when the amount of starch or cereal meal fed at the same time was increased.


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