Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis
Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we prov...
Gespeichert in:
| Veröffentlicht in: | Biochemical journal 2008-10, Vol.415 (1), p.27-33 |
|---|---|
| Hauptverfasser: | , |
| Format: | Artikel |
| Sprache: | eng |
| Schlagworte: | |
| Online-Zugang: | Volltext |
| Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
| container_end_page | 33 |
|---|---|
| container_issue | 1 |
| container_start_page | 27 |
| container_title | Biochemical journal |
| container_volume | 415 |
| creator | Thakur, Meghna Chakraborti, Pradip K |
| description | Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we provide the evidence for the ability of PknA to transphosphorylate mMurD (mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate-ligase), the enzyme involved in peptidoglycan biosynthesis. Its co-expression in Escherichia coli along with PknA resulted in phosphorylation of mMurD. Consistent with these observations, results of the solid-phase binding assays revealed a high-affinity in vitro binding between the two proteins. Furthermore, overexpression of m-murD in Mycobacterium smegmatis yielded a phosphorylated protein. The results of the present study therefore point towards the possibility of mMurD being a substrate of PknA. |
| doi_str_mv | 10.1042/bj20080234 |
| format | Article |
| fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_69524020</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>69524020</sourcerecordid><originalsourceid>FETCH-LOGICAL-c351t-4951f16be685b6b31dd30380fd24a1358a334b2e1f6d06b077a967d003a6841a3</originalsourceid><addsrcrecordid>eNpFkc9u1DAQxi0EotvChQdAPnFADR3_iZM9LoVCq1ZwgHNkJ5Ouu1472E6lvA8Pildd1MNoPo1--mY0HyHvGHxiIPmFeeAALXAhX5AVkw1UbcPbl2QFXMlKAWcn5DSlBwAmQcJrcsLaum4akCvyd2Oss3mhYaQ_d35zTjXdL30wus8YrXYU552OS8i2r_IyIU1l7PEibyMGXxTdWa8TntMcaI7ap2kbDhUXpzPSuzl-OZg6e18oav1jcI84FEHzFukUQ48pHdZPOGU7hHu39NpTY0NafEGSTW_Iq1G7hG-P_Yz8vvr66_J7dfvj2_Xl5rbqRc1yJdc1G5kyqNraKCPYMAgQLYwDl5qJutVCSMORjWoAZaBp9Fo1A4DQqpVMizPy4cm3XPVnxpS7vU09Oqc9hjl1al1zCRwK-PEJ7GNIKeLYTdHuy5s6Bt0hk-7zzf9MCvz-6DqbPQ7P6DEE8Q8S8ImW</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>69524020</pqid></control><display><type>article</type><title>Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis</title><source>MEDLINE</source><source>Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals</source><source>PubMed Central</source><creator>Thakur, Meghna ; Chakraborti, Pradip K</creator><creatorcontrib>Thakur, Meghna ; Chakraborti, Pradip K</creatorcontrib><description>Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we provide the evidence for the ability of PknA to transphosphorylate mMurD (mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate-ligase), the enzyme involved in peptidoglycan biosynthesis. Its co-expression in Escherichia coli along with PknA resulted in phosphorylation of mMurD. Consistent with these observations, results of the solid-phase binding assays revealed a high-affinity in vitro binding between the two proteins. Furthermore, overexpression of m-murD in Mycobacterium smegmatis yielded a phosphorylated protein. The results of the present study therefore point towards the possibility of mMurD being a substrate of PknA.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj20080234</identifier><identifier>PMID: 18557704</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Bacterial Proteins - physiology ; Molecular Sequence Data ; Mycobacterium smegmatis - metabolism ; Peptide Synthases - metabolism ; Phosphorylation ; Protein-Serine-Threonine Kinases - physiology ; Sequence Alignment ; Two-Hybrid System Techniques</subject><ispartof>Biochemical journal, 2008-10, Vol.415 (1), p.27-33</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c351t-4951f16be685b6b31dd30380fd24a1358a334b2e1f6d06b077a967d003a6841a3</citedby><cites>FETCH-LOGICAL-c351t-4951f16be685b6b31dd30380fd24a1358a334b2e1f6d06b077a967d003a6841a3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/18557704$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Thakur, Meghna</creatorcontrib><creatorcontrib>Chakraborti, Pradip K</creatorcontrib><title>Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we provide the evidence for the ability of PknA to transphosphorylate mMurD (mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate-ligase), the enzyme involved in peptidoglycan biosynthesis. Its co-expression in Escherichia coli along with PknA resulted in phosphorylation of mMurD. Consistent with these observations, results of the solid-phase binding assays revealed a high-affinity in vitro binding between the two proteins. Furthermore, overexpression of m-murD in Mycobacterium smegmatis yielded a phosphorylated protein. The results of the present study therefore point towards the possibility of mMurD being a substrate of PknA.</description><subject>Amino Acid Sequence</subject><subject>Bacterial Proteins - physiology</subject><subject>Molecular Sequence Data</subject><subject>Mycobacterium smegmatis - metabolism</subject><subject>Peptide Synthases - metabolism</subject><subject>Phosphorylation</subject><subject>Protein-Serine-Threonine Kinases - physiology</subject><subject>Sequence Alignment</subject><subject>Two-Hybrid System Techniques</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2008</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNpFkc9u1DAQxi0EotvChQdAPnFADR3_iZM9LoVCq1ZwgHNkJ5Ouu1472E6lvA8Pildd1MNoPo1--mY0HyHvGHxiIPmFeeAALXAhX5AVkw1UbcPbl2QFXMlKAWcn5DSlBwAmQcJrcsLaum4akCvyd2Oss3mhYaQ_d35zTjXdL30wus8YrXYU552OS8i2r_IyIU1l7PEibyMGXxTdWa8TntMcaI7ap2kbDhUXpzPSuzl-OZg6e18oav1jcI84FEHzFukUQ48pHdZPOGU7hHu39NpTY0NafEGSTW_Iq1G7hG-P_Yz8vvr66_J7dfvj2_Xl5rbqRc1yJdc1G5kyqNraKCPYMAgQLYwDl5qJutVCSMORjWoAZaBp9Fo1A4DQqpVMizPy4cm3XPVnxpS7vU09Oqc9hjl1al1zCRwK-PEJ7GNIKeLYTdHuy5s6Bt0hk-7zzf9MCvz-6DqbPQ7P6DEE8Q8S8ImW</recordid><startdate>20081001</startdate><enddate>20081001</enddate><creator>Thakur, Meghna</creator><creator>Chakraborti, Pradip K</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope></search><sort><creationdate>20081001</creationdate><title>Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis</title><author>Thakur, Meghna ; Chakraborti, Pradip K</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c351t-4951f16be685b6b31dd30380fd24a1358a334b2e1f6d06b077a967d003a6841a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2008</creationdate><topic>Amino Acid Sequence</topic><topic>Bacterial Proteins - physiology</topic><topic>Molecular Sequence Data</topic><topic>Mycobacterium smegmatis - metabolism</topic><topic>Peptide Synthases - metabolism</topic><topic>Phosphorylation</topic><topic>Protein-Serine-Threonine Kinases - physiology</topic><topic>Sequence Alignment</topic><topic>Two-Hybrid System Techniques</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Thakur, Meghna</creatorcontrib><creatorcontrib>Chakraborti, Pradip K</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Thakur, Meghna</au><au>Chakraborti, Pradip K</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2008-10-01</date><risdate>2008</risdate><volume>415</volume><issue>1</issue><spage>27</spage><epage>33</epage><pages>27-33</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>Eukaryotic-type serine/threonine protein kinases in bacteria have been implicated in controlling a host of cellular activities. PknA is one of eleven such protein kinases from Mycobacterium tuberculosis which regulates morphological changes associated with cell division. In the present study we provide the evidence for the ability of PknA to transphosphorylate mMurD (mycobacterial UDP-N-acetylmuramoyl-L-alanine:D-glutamate-ligase), the enzyme involved in peptidoglycan biosynthesis. Its co-expression in Escherichia coli along with PknA resulted in phosphorylation of mMurD. Consistent with these observations, results of the solid-phase binding assays revealed a high-affinity in vitro binding between the two proteins. Furthermore, overexpression of m-murD in Mycobacterium smegmatis yielded a phosphorylated protein. The results of the present study therefore point towards the possibility of mMurD being a substrate of PknA.</abstract><cop>England</cop><pmid>18557704</pmid><doi>10.1042/bj20080234</doi><tpages>7</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0264-6021 |
| ispartof | Biochemical journal, 2008-10, Vol.415 (1), p.27-33 |
| issn | 0264-6021 1470-8728 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_69524020 |
| source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
| subjects | Amino Acid Sequence Bacterial Proteins - physiology Molecular Sequence Data Mycobacterium smegmatis - metabolism Peptide Synthases - metabolism Phosphorylation Protein-Serine-Threonine Kinases - physiology Sequence Alignment Two-Hybrid System Techniques |
| title | Ability of PknA, a mycobacterial eukaryotic-type serine/threonine kinase, to transphosphorylate MurD, a ligase involved in the process of peptidoglycan biosynthesis |
| url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-04T09%3A30%3A10IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Ability%20of%20PknA,%20a%20mycobacterial%20eukaryotic-type%20serine/threonine%20kinase,%20to%20transphosphorylate%20MurD,%20a%20ligase%20involved%20in%20the%20process%20of%20peptidoglycan%20biosynthesis&rft.jtitle=Biochemical%20journal&rft.au=Thakur,%20Meghna&rft.date=2008-10-01&rft.volume=415&rft.issue=1&rft.spage=27&rft.epage=33&rft.pages=27-33&rft.issn=0264-6021&rft.eissn=1470-8728&rft_id=info:doi/10.1042/bj20080234&rft_dat=%3Cproquest_cross%3E69524020%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=69524020&rft_id=info:pmid/18557704&rfr_iscdi=true |