Essential arginyl residues in Escherichia coli alkaline phosphatase

Daemen, F.J.M.; Riordan, James

doi:10.1021/bi00711a014

Cited by 97 publications

(41 citation statements)

References 26 publications

(16 reference statements)

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“…In agreement with other studies [16,17,201, reactivation at room temperature is a slow process. After 16 h of reactivation the activity increases from 65 to 75 for the protein sample inactivated with 2,3-butanedione for 10 min, and from 30 % to 60 % for the protein sample inactivated for 30 min of treatment.…”

Section: Modification With 23-butanedionesupporting

confidence: 93%

Modification of the Phosphatidylcholine‐Transfer Protein from Bovine Liver with Butanedione and Phenyiglyoxal

Akeroyd

Lange

Westerman

et al. 1981

European Journal of Biochemistry

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Modification of arginine residues with 2,3‐butanedione and phenylglyoxal completely inhibits the transfer activity of the phosphatidylcholine transfer protein from bovine liver. Removal of borate and butanedione leads to a slow reactivation of the protein. Both α‐dicarbonyl reagents modify three of the ten arginine residues present per protein molecule. The extent of modification is linearly related to the loss of activity. Inactivation with butanedione is greatly diminished when the protein is bound to strongly negatively charged vesicles. Under these conditions a rapid modification of two arginine residues is observed. This suggests that the transfer protein contains one arginine residue essential for activity, probably as a binding site for the negatively charged phosphate group of the phosphatidylcholine molecule. This study provides convincing evidence that arginine residues may play an essential role in phospholipid‐ protein interactions.

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Section: Modification With 23-butanedionesupporting

confidence: 93%

Modification of the Phosphatidylcholine‐Transfer Protein from Bovine Liver with Butanedione and Phenyiglyoxal

Akeroyd

Lange

Westerman

et al. 1981

European Journal of Biochemistry

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“…An arginine residue can serve as the binding site for anionic phosphorylated ligands as well as for anionic nucleotide coenzymes (30)(31)(32)(33)(34)(35). Thus, arginines are critical for substrate binding to a wide range of enzymes.…”

Section: Resultsmentioning

confidence: 99%

An essential arginine residue for initiation of protein-primed DNA replication.

Hsieh

Yoo

Ito

1990

Proc. Natl. Acad. Sci. U.S.A.

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A group of proteins that act as primers for initiation of linear DNA replication are called DNA-terminal proteins (terminal proteins). We have found a short stretch of conserved amino acid sequence among the terminal proteins from six different sources. The location of this sequence motif is also similar among the different terminal proteins. To determine the functional role of this terminal-protein domain in DNA replication, we have studied the bacteriophage PRD1 system. The PRD1 terminal protein and DNA polymerase genes were cloned into expression vectors, and the recombinant plasmids were used for constructing PRD1 terminal protein mutants. Site-directed mutagenesis and functional analysis showed that one of the two arginines Because DNA polymerases require template and primer and act only in the 5' to 3' direction, linear double-stranded DNA genomes pose the special problem of preserving the 5' ends of DNA during DNA replication (1). If RNA molecules are used as primers and are removed, gaps will be created at the 5' ends and will never be filled (1). Several viral genomes use proteins, instead of RNAs, as primers for the initiation of DNA replication (2-6). Such proteins not only function as the primers for DNA synthesis but also remain bound to the 5' ends of DNA and are encapsulated during viral morphogenesis. These proteins bound to the DNA then can be isolated as covalent DNA-protein complexes from viral particles. Thus, they have been called DNA-terminal proteins or simply terminal proteins.The "protein-priming" mechanism for the initiation of DNA replication involves in principle the deoxynucleotidylation of a hydroxy amino acid residue within the terminal protein. The hydroxy amino acid can be serine (7,8), threonine (9), or tyrosine (10). This deoxynucleotidylation is catalyzed by virus-encoded DNA polymerases and is dependent on the presence of Mg2' and the viral DNA-protein complex as a template. The consequent terminal proteindNMP complex is then used to initiate chain elongation.Bacteriophage PRD1 is a small lipid-containing phage that infects a wide variety of Gram-negative bacteria (11). The genome of PRD1 is a linear, double-stranded DNA molecule of'14.7 kilobase pairs (kb) and has a 28-kDa terminal protein linked covalently to each 5' terminus (11). The linkage between the terminal protein and DNA is a phosphodiester bond between the hydroxyl group of a tyrosine residue of the terminal protein and a dGMP nucleotide at the 5' terminus of the PRD1 DNA (10).The nucleotide sequence ofthe PRD1 terminal protein gene has been described (12, 13). When the deduced amino acid sequence was compared with those of other terminal proteins previously reported, no substantial amino acid sequence homology was found (12, 13). On the other hand, the PRD1 DNA polymerase showed significant sequence homology not only with the other protein-primed DNA polymerases but also with RNA-primed DNA polymerases. These observations strongly suggest that both protein-primed and RNAprimed DNA polymerases have evolv...

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“…In order to examine the effect of Arg residues in DNA recognition we chemically modified these residues with 2,3-butanedione. This modifying agent reacts with arginine to yield a dihydroxyimidazoline derivative (13). We have found that 2,3-butanedione at a concentration of 0.4 mM completely abolishes MmeI endonucleolytic activity (Fig.…”

Section: Vol 75 2009 Analysis Of the Mmei Restriction-modification mentioning

confidence: 94%

Functional Analysis of MmeI from Methanol UtilizerMethylophilus methylotrophus, a Subtype IIC Restriction-Modification Enzyme Related to Type I Enzymes

Nakonieczna

Kaczorowski

Obarska-Kosińska

et al. 2009

Appl Environ Microbiol

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MmeI from6 -adenine ␥-class DNA methyltransferases; (iii) the C-terminal portion (aa 610 to 919) containing a putative target recognition domain. Interestingly, all three domains showed highest similarity to the corresponding elements of type I enzymes rather than to classical type II enzymes. We have found that MmeI variants deficient in restriction activity (D70A, E80A, and K82A) can bind and methylate specific nucleotide sequence. This suggests that domains of MmeI responsible for DNA restriction and modification can act independently. Moreover, we have shown that a single amino acid residue substitution within the putative target recognition domain (S807A) resulted in a MmeI variant with a higher endonucleolytic activity than the wild-type enzyme.Restriction-modification (RM) systems are composed of two enzymatic entities: a restriction endodeoxyribonuclease (REase) that cleaves DNA usually within short, specific sequences and a methyltransferase (MTase) that modifies the same sequence in order to protect the host genomic DNA against the action of the cognate restriction enzyme. Based on their molecular structure, functional features, and cofactors requirements, RM systems can be divided into four distinct types (49). The most complex are enzymes of types I and III (and some of type IV), which function as multisubunit molecular machines that exhibit very complex mechanism of action involving NTP hydrolysis and DNA translocation (reviewed in reference 4). On the other hand, type II RM systems comprise relatively simple independent REase and MTase enzymes whose properties, in particular recognition of short specific nucleotide sequences (4 to 8 bp), have made them indispensable tools of modern molecular biology (45). To date, almost 4,000 type II REases have been identified by screening various Bacteria, Archaea, and viruses and characterizing them biochemically (50).DNA MTases of RM systems belong to several different families within the Rossmann fold methyltransferase superfamily (6). Structural conservation is strong across catalytic domains of all DNA MTases, despite sequence divergence between families and frequent fusions with additional, unrelated domains that are involved in, for example, specific recognition of the target DNA sequence (29). Two major families are the m 5 C MTases, a group of proteins with high mutual sequence similarity and only remote similarity to other MTases (48), and the N-MTases (m 6 A and m 4 C MTases), a large and heterogeneous group of enzymes that exhibit very complex mutual relationships (9,34). The N-MTase family contains not only type II enzymes, but also MTase subunits

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Essential arginyl residues in Escherichia coli alkaline phosphatase

Cited by 97 publications

References 26 publications

Modification of the Phosphatidylcholine‐Transfer Protein from Bovine Liver with Butanedione and Phenyiglyoxal

Modification of the Phosphatidylcholine‐Transfer Protein from Bovine Liver with Butanedione and Phenyiglyoxal

An essential arginine residue for initiation of protein-primed DNA replication.

Functional Analysis of MmeI from Methanol UtilizerMethylophilus methylotrophus, a Subtype IIC Restriction-Modification Enzyme Related to Type I Enzymes

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