| Title |
Effect of conserved intersubunit amino acid substitutions on Hfq protein structure and stability
|
|---|---|
| Published in |
Biochemistry, May 2014
|
| DOI | 10.1134/s0006297914050113 |
| Pubmed ID | |
| Authors |
V. N. Murina, B. S. Melnik, V. V. Filimonov, M. Ühlein, M. S. Weiss, U. Müller, A. D. Nikulin |
| Abstract |
Hfq is a thermostable RNA-binding bacterial protein that forms a uniquely shaped homohexamer. Based on sequence and structural similarity, Hfq belongs to the like-Sm (LSm) protein family. In spite of a rather high degree of homology between archaeal and eukaryotic LSm proteins, their quaternary structure is different, usually consisting of five to eight monomers. In this work, the importance of conserved intersubunit hydrogen bonds for the Hfq spatial organization was tested. The structures and stabilities for the Gln8Ala, Asn28Ala, Asp40Ala, and Tyr55Ala Hfq mutants were determined. All these proteins have the same hexamer organization, but their stability is different. Elimination of a single intersubunit hydrogen bond due to Gln8Ala, Asp40Ala, and Tyr55Ala substitutions results in decreased stability of the Hfq hexamer. Tyr55Ala Hfq as well as the earlier studied His57Ala Hfq has reduced protein thermostability, which seems to correspond to an opening of the protein hydrophobic core. |
X Demographics
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Geographical breakdown
| Country | Count | As % |
|---|---|---|
| Unknown | 1 | 100% |
Demographic breakdown
| Type | Count | As % |
|---|---|---|
| Members of the public | 1 | 100% |
Mendeley readers
The data shown below were compiled from readership statistics for 26 Mendeley readers of this research output. Click here to see the associated Mendeley record.
Geographical breakdown
| Country | Count | As % |
|---|---|---|
| India | 1 | 4% |
| United States | 1 | 4% |
| Russia | 1 | 4% |
| Unknown | 23 | 88% |
Demographic breakdown
| Readers by professional status | Count | As % |
|---|---|---|
| Student > Ph. D. Student | 10 | 38% |
| Researcher | 5 | 19% |
| Student > Bachelor | 4 | 15% |
| Student > Doctoral Student | 2 | 8% |
| Professor | 1 | 4% |
| Other | 2 | 8% |
| Unknown | 2 | 8% |
| Readers by discipline | Count | As % |
|---|---|---|
| Biochemistry, Genetics and Molecular Biology | 13 | 50% |
| Agricultural and Biological Sciences | 8 | 31% |
| Chemistry | 1 | 4% |
| Unknown | 4 | 15% |
Attention Score in Context
This research output has an Altmetric Attention Score of 1. This is our high-level measure of the quality and quantity of online attention that it has received. This Attention Score, as well as the ranking and number of research outputs shown below, was calculated when the research output was last mentioned on 07 February 2015.
All research outputs
#17,285,036
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Outputs from Biochemistry
#19,491
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Outputs of similar age
#145,899
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Outputs of similar age from Biochemistry
#54
of 96 outputs
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