The importance of C-terminal aspartic acid residue (D141) to the antirestriction activity of the ArdB (R64) protein
Antirestriction proteins of the ArdB/KlcA family are specific inhibitors of restriction (endonuclease) activity of type-I restriction/modification enzymes. The effect of conserved amino acid residues on the antirestriction activity of the ArdB protein encoded by the transmissible R64 (IncI1) plasmid has been investigated. An analysis of the amino acid sequences of ArdB homologues demonstrated the presence of four groups of conserved residues ((1) R16, E32, and W51; (2) Y46 and G48; (3) S81, D83 and E132, and (4) N77, L(I)140, and D141) on the surface of the protein globule. Amino acid residues of the fourth group showed a unique localization pattern with the terminal residue protruding beyond the globule surface. The replacement of two conserved amino acids (D141 and N77) located in the close vicinity of each other on the globule surface showed that the C-terminal D141 is essential for the antirestriction activity of ArdB. The deletion of this residue, as well as replacement by a hydrophobic threonine residue (D141T), completely abolished the antirestriction activity of ArdB. The synonymous replacement of D141 by a glutamic acid residue (D141E) caused an approximately 30-fold decrease of the antirestriction activity of ArdB, and the point mutation N77A caused an approximately 20-fold decrease in activity. The residues D141 and N77 located on the surface of the protein globule are presumably essential for the formation of a contact between ArdB and a currently unknown factor that modulates the activity of type-I restriction/modification enzymes.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2017 |
|---|---|
| Erschienen: |
2017 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:51 |
|---|---|
| Enthalten in: |
Molekuliarnaia biologiia - 51(2017), 5 vom: 16. Sept., Seite 831-835 |
| Sprache: |
Russisch |
|---|
| Beteiligte Personen: |
Kudryavtseva, A A [VerfasserIn] |
|---|
| Links: |
|---|
| Themen: |
30KYC7MIAI |
|---|
| Anmerkungen: |
Date Completed 11.06.2018 Date Revised 11.06.2018 published: Print Citation Status MEDLINE |
|---|
| doi: |
10.7868/S002689841705010X |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM277830400 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM277830400 | ||
| 003 | DE-627 | ||
| 005 | 20231225015201.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231225s2017 xx |||||o 00| ||rus c | ||
| 024 | 7 | |a 10.7868/S002689841705010X |2 doi | |
| 028 | 5 | 2 | |a pubmed24n0926.xml |
| 035 | |a (DE-627)NLM277830400 | ||
| 035 | |a (NLM)29116070 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a rus | ||
| 100 | 1 | |a Kudryavtseva, A A |e verfasserin |4 aut | |
| 245 | 1 | 4 | |a The importance of C-terminal aspartic acid residue (D141) to the antirestriction activity of the ArdB (R64) protein |
| 264 | 1 | |c 2017 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 11.06.2018 | ||
| 500 | |a Date Revised 11.06.2018 | ||
| 500 | |a published: Print | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a Antirestriction proteins of the ArdB/KlcA family are specific inhibitors of restriction (endonuclease) activity of type-I restriction/modification enzymes. The effect of conserved amino acid residues on the antirestriction activity of the ArdB protein encoded by the transmissible R64 (IncI1) plasmid has been investigated. An analysis of the amino acid sequences of ArdB homologues demonstrated the presence of four groups of conserved residues ((1) R16, E32, and W51; (2) Y46 and G48; (3) S81, D83 and E132, and (4) N77, L(I)140, and D141) on the surface of the protein globule. Amino acid residues of the fourth group showed a unique localization pattern with the terminal residue protruding beyond the globule surface. The replacement of two conserved amino acids (D141 and N77) located in the close vicinity of each other on the globule surface showed that the C-terminal D141 is essential for the antirestriction activity of ArdB. The deletion of this residue, as well as replacement by a hydrophobic threonine residue (D141T), completely abolished the antirestriction activity of ArdB. The synonymous replacement of D141 by a glutamic acid residue (D141E) caused an approximately 30-fold decrease of the antirestriction activity of ArdB, and the point mutation N77A caused an approximately 20-fold decrease in activity. The residues D141 and N77 located on the surface of the protein globule are presumably essential for the formation of a contact between ArdB and a currently unknown factor that modulates the activity of type-I restriction/modification enzymes | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Antirestriction | |
| 650 | 4 | |a ArdB | |
| 650 | 4 | |a R64 | |
| 650 | 4 | |a transmissible plasmid | |
| 650 | 7 | |a Escherichia coli Proteins |2 NLM | |
| 650 | 7 | |a ardB protein, E coli |2 NLM | |
| 650 | 7 | |a Aspartic Acid |2 NLM | |
| 650 | 7 | |a 30KYC7MIAI |2 NLM | |
| 650 | 7 | |a Deoxyribonucleases, Type I Site-Specific |2 NLM | |
| 650 | 7 | |a EC 3.1.21.3 |2 NLM | |
| 700 | 1 | |a Osetrova, M S |e verfasserin |4 aut | |
| 700 | 1 | |a Livinyuk, V Ya |e verfasserin |4 aut | |
| 700 | 1 | |a Manukhov, I V |e verfasserin |4 aut | |
| 700 | 1 | |a Zavilgelsky, G B |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t Molekuliarnaia biologiia |d 1975 |g 51(2017), 5 vom: 16. Sept., Seite 831-835 |w (DE-627)NLM000033979 |x 0026-8984 |7 nnns |
| 773 | 1 | 8 | |g volume:51 |g year:2017 |g number:5 |g day:16 |g month:09 |g pages:831-835 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.7868/S002689841705010X |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 51 |j 2017 |e 5 |b 16 |c 09 |h 831-835 | ||