Amino Acid Residues That Influence the Binding of Manganese or Calcium to Photosystem II. 2. The Carboxy-Terminal Domain of the D1 Polypeptide

Biochemistry ◽  
1995 ◽  
Vol 34 (17) ◽  
pp. 5859-5882 ◽  
Author(s):  
Hsiu-An Chu ◽  
Anh P. Nguyen ◽  
Richard J. Debus
Keyword(s):  
Amino Acid ◽  
Photosystem Ii ◽  
Amino Acid Residues ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
D1 Polypeptide ◽  
Carboxy Terminal

scholarly journals THE STRUCTURAL BASIS FOR BINDING OF COMPLEMENT BY IMMUNOGLOBULIN M

1974 ◽  
Vol 140 (4) ◽  
pp. 1117-1121 ◽  
Author(s):  
Mary M. Hurst ◽  
John E. Volanakis ◽  
Raymond B. Hester ◽  
Robert M. Stroud ◽  
J. Claude Bennett
Keyword(s):  
Amino Acid ◽  
Structural Features ◽  
Immunoglobulin M ◽  
Structural Basis ◽  
Amino Acid Residues ◽  
Amino Terminal ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Carboxy Terminal ◽  
Insight Into

An insight into the structural features of human IgM that are responsible for its capacity to bind the first component of complement (C) has been obtained by examining the ability of IgM subfragments to bind active C1 (C1). The smallest two fragments found to bind C1 were the major CNBr fragment of the Fc portion of IgM and the CH4 fragment of the carboxy-terminal domain. The smallest fragment which fixes C1 has a disaggregated mol wt of 6,800, consists of 60 residues, and contains no carbohydrate. Structural considerations and sequence overlaps suggest that the amino-terminal side of the CH4 domain (24 amino acid residues) might be responsible for fixing C1.

scholarly journals Alternatively spliced forms in the carboxy-terminal domain of the p53 protein regulate its ability to promote annealing of complementary single strands of nucleic acids.

1995 ◽  
Vol 15 (1) ◽  
pp. 497-504 ◽  
Author(s):  
L Wu ◽  
J H Bayle ◽  
B Elenbaas ◽  
N P Pavletich ◽  
A J Levine
Keyword(s):  
Amino Acid ◽  
Alternative Splice ◽  
P53 Protein ◽  
Amino Acid Residues ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Alternatively Spliced ◽  
Carboxy Terminal ◽  
Splice Forms ◽  
Cancerous Cells

The carboxy-terminal domain of the p53 protein comprising amino acid residues 311 to 393 is able to promote the reassociation of single-stranded RNA or DNA into duplex hybrids. This domain is as efficient as the intact p53 protein in both the rate and the extent of the double-stranded product produced in this reaction. Both wild-type and mutant p53 proteins from cancerous cells carry out this reaction. The monoclonal antibody PAb421, which detects an epitope between residues 370 and 378, blocks the ability of p53 to reassociate single strands of RNA or DNA. Similarly, the alternative splice form of the murine p53 protein, which removes amino acid residues 364 to 390 and replaces them with 17 new amino acids, does not carry out the reassociation reaction with RNA or DNA. This is the first indication of functionally distinct properties of the alternative splice forms of p53. These results suggest that this splice alternative can regulate a p53-mediated reaction that may be related to the functions of this protein.

scholarly journals Exploring the Ability of LARS2 Carboxy-Terminal Domain in Rescuing the MELAS Phenotype

Life ◽  
2021 ◽  
Vol 11 (7) ◽  
pp. 674
Author(s):  
Francesco Capriglia ◽  
Francesca Rizzo ◽  
Giuseppe Petrosillo ◽  
Veronica Morea ◽  
Giulia d’Amati ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Molecular Mechanisms ◽  
Mitochondrial Protein ◽  
Trna Synthetase ◽  
Mitochondrial Protein Synthesis ◽  
Mitochondrial Translation ◽  
Terminal Domain ◽  
Carboxy Terminal Domain ◽  
Mitochondrial Functions ◽  
Carboxy Terminal

The m.3243A>G mutation within the mitochondrial mt-tRNALeu(UUR) gene is the most prevalent variant linked to mitochondrial encephalopathy with lactic acidosis and stroke-like episodes (MELAS) syndrome. This pathogenic mutation causes severe impairment of mitochondrial protein synthesis due to alterations of the mutated tRNA, such as reduced aminoacylation and a lack of post-transcriptional modification. In transmitochondrial cybrids, overexpression of human mitochondrial leucyl-tRNA synthetase (LARS2) has proven effective in rescuing the phenotype associated with m.3243A>G substitution. The rescuing activity resides in the carboxy-terminal domain (Cterm) of the enzyme; however, the precise molecular mechanisms underlying this process have not been fully elucidated. To deepen our knowledge on the rescuing mechanisms, we demonstrated the interactions of the Cterm with mutated mt-tRNALeu(UUR) and its precursor in MELAS cybrids. Further, the effect of Cterm expression on mitochondrial functions was evaluated. We found that Cterm ameliorates de novo mitochondrial protein synthesis, whilst it has no effect on mt-tRNALeu(UUR) steady-state levels and aminoacylation. Despite the complete recovery of cell viability and the increase in mitochondrial translation, Cterm-overexpressing cybrids were not able to recover bioenergetic competence. These data suggest that, in our MELAS cell model, the beneficial effect of Cterm may be mediated by factors that are independent of the mitochondrial bioenergetics.

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