DOI: 10.1046/j.1432-1327.2000.01380.x. Structural requirements for thymosin β4 in its contact with actin

Structural requirements for thymosin β4 in its contact with actin

10.1046/j.1432-1327.2000.01380.x

Crossref journal-article

Wiley

European Journal of Biochemistry (311)

Abstract

We examined the conformational preferences of mutants of thymosin β4, an actin monomer sequestering protein by NMR spectroscopy in 60% (v/v) trifluoroethanol. Under these conditions, the wild‐type thymosin β4 conformation consists of an α‐helix (helix I) extending from residues 5–16 with a more stable fragment from lysine 11 to lysine 16 and a second α‐helix (helix II) encompassing residues 31–39. The point mutations studied here are located in helix I or in the LKKTET segment (residues 17–22) that form the two main entities of interaction with the actin molecule. The α‐1H conformational shifts allow us to investigate the helicity of the polypeptides at the residue level and to correlate these structures with their biological activity. We determine that an extension of helix I at its C‐terminal end over the LKK‐segment results in loss of activity. The correct termination of this helix is connected to a specific orientation of the polypeptide essential for a cooperative action of the thymosin β4 binding entities required for full activity.

Bibliography

Simenel, C., Van Troys, M., Vandekerckhove, J., Ampe, C., & Delepierre, M. (2000). Structural requirements for thymosin Î²4 in its contact with actin. European Journal of Biochemistry, 267(12), 3530â3538. Portico.

Authors 5

Catherine Simenel (first)
Marleen Van Troys (additional)
Joël Vandekerckhove (additional)
Christophe Ampe (additional)
Muriel Delepierre (additional)

References 38 Referenced 23

10.1083/jcb.123.1.1
10.1016/S0021-9258(20)64278-8 / J. Biol. Chem. / Thymosin β4 and Fx, an actin sequestering peptide are undistinguishable by Safer D. (1991)
10.1016/0092-8674(93)90544-Z
10.1021/bi00486a006
10.1111/j.1432-1033.1993.tb18382.x
10.1021/bi970185v
10.1002/j.1460-2075.1992.tb05579.x
10.1002/j.1460-2075.1996.tb00350.x
10.1023/A:1026317612554
10.1016/S0167-4889(98)00152-9
10.1016/S0021-9258(18)62016-2
10.1016/0022-2364(82)90279-7
10.1016/0006-291X(83)91225-1
10.1021/ja00231a044
10.1016/0022-2364(85)90018-6
10.1016/0022-2364(81)90037-8
10.1023/A:1018315729609
10.1016/0014-5793(87)80948-1
10.1016/0022-2364(89)90341-7
10.1002/bip.360291009
10.1016/0022-2836(91)90214-Q
10.1016/S0076-6879(94)39014-2
10.1146/annurev.bi.47.070178.001343
10.1038/nsb0694-399
10.1006/jmbi.1994.0023
10.1006/jmbi.1994.0024
10.1006/bbrc.1996.0693
10.1021/bi00152a015
10.1051/epn/19861701011
10.1007/BF00227466
10.1007/BF00227471
10.1021/bi00069a025
10.1126/science.3381086
10.1111/j.1399-3011.1993.tb00470.x
10.1126/science.8178170
10.1006/jmbi.1997.1322
10.1111/j.1399-3011.1995.tb01322.x
10.1038/nsb0397-180

Dates

Type	When
Created	22 years, 5 months ago (March 11, 2003, 7:47 a.m.)
Deposited	1 year, 10 months ago (Oct. 15, 2023, 9:17 p.m.)
Indexed	11 months, 1 week ago (Sept. 15, 2024, 3:33 p.m.)
Issued	25 years, 2 months ago (June 1, 2000)
Published	25 years, 2 months ago (June 1, 2000)
Published Online	22 years ago (Aug. 18, 2003)
Published Print	25 years, 2 months ago (June 1, 2000)

Funders 0

None

BibTeX

@article{Simenel_2000, title={Structural requirements for thymosin β4 in its contact with actin: An NMR‐analysis of thymosin β4 mutants in solution and correlation with their biological activity}, volume={267}, ISSN={1432-1033}, url={http://dx.doi.org/10.1046/j.1432-1327.2000.01380.x}, DOI={10.1046/j.1432-1327.2000.01380.x}, number={12}, journal={European Journal of Biochemistry}, publisher={Wiley}, author={Simenel, Catherine and Van Troys, Marleen and Vandekerckhove, Joël and Ampe, Christophe and Delepierre, Muriel}, year={2000}, month=jun, pages={3530–3538} }

JSON

{
  "indexed": {
    "date-parts": [
      [
        2024,
        9,
        15
      ]
    ],
    "date-time": "2024-09-15T19:33:38Z",
    "timestamp": 1726428818897
  },
  "reference-count": 38,
  "publisher": "Wiley",
  "issue": "12",
  "license": [
    {
      "start": {
        "date-parts": [
          [
            2003,
            8,
            18
          ]
        ],
        "date-time": "2003-08-18T00:00:00Z",
        "timestamp": 1061164800000
      },
      "content-version": "vor",
      "delay-in-days": 1173,
      "URL": "http://onlinelibrary.wiley.com/termsAndConditions#vor"
    }
  ],
  "content-domain": {
    "domain": [],
    "crossmark-restriction": false
  },
  "published-print": {
    "date-parts": [
      [
        2000,
        6
      ]
    ]
  },
  "abstract": "<jats:p>We examined the conformational preferences of mutants of thymosin\u2003\u03b24, an actin monomer sequestering protein by NMR spectroscopy in 60% (v/v) trifluoroethanol. Under these conditions, the wild\u2010type thymosin\u2003\u03b24 conformation consists of an \u03b1\u2010helix (helix\u2003I) extending from residues 5\u201316 with a more stable fragment from lysine 11 to lysine 16 and a second \u03b1\u2010helix (helix\u2003II) encompassing residues 31\u201339. The point mutations studied here are located in helix\u2003I or in the LKKTET segment (residues 17\u201322) that form the two main entities of interaction with the actin molecule. The \u03b1\u2010<jats:sup>1</jats:sup>H conformational shifts allow us to investigate the helicity of the polypeptides at the residue level and to correlate these structures with their biological activity. We determine that an extension of helix\u2003I at its C\u2010terminal end over the LKK\u2010segment results in loss of activity. The correct termination of this helix is connected to a specific orientation of the polypeptide essential for a cooperative action of the thymosin\u2003\u03b24 binding entities required for full activity.</jats:p>",
  "DOI": "10.1046/j.1432-1327.2000.01380.x",
  "type": "journal-article",
  "created": {
    "date-parts": [
      [
        2003,
        3,
        11
      ]
    ],
    "date-time": "2003-03-11T12:47:16Z",
    "timestamp": 1047386836000
  },
  "page": "3530-3538",
  "source": "Crossref",
  "is-referenced-by-count": 23,
  "title": "Structural requirements for thymosin \u03b24 in its contact with actin",
  "prefix": "10.1111",
  "volume": "267",
  "author": [
    {
      "given": "Catherine",
      "family": "Simenel",
      "sequence": "first",
      "affiliation": []
    },
    {
      "given": "Marleen",
      "family": "Van Troys",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Jo\u00ebl",
      "family": "Vandekerckhove",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Christophe",
      "family": "Ampe",
      "sequence": "additional",
      "affiliation": []
    },
    {
      "given": "Muriel",
      "family": "Delepierre",
      "sequence": "additional",
      "affiliation": []
    }
  ],
  "member": "311",
  "published-online": {
    "date-parts": [
      [
        2003,
        8,
        18
      ]
    ]
  },
  "reference": [
    {
      "key": "e_1_2_8_2_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1083/jcb.123.1.1"
    },
    {
      "key": "e_1_2_8_3_2",
      "doi-asserted-by": "crossref",
      "first-page": "4029",
      "DOI": "10.1016/S0021-9258(20)64278-8",
      "article-title": "Thymosin \u03b24 and Fx, an actin sequestering peptide are undistinguishable",
      "volume": "266",
      "author": "Safer D.",
      "year": "1991",
      "journal-title": "J. Biol. Chem."
    },
    {
      "key": "e_1_2_8_4_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0092-8674(93)90544-Z"
    },
    {
      "key": "e_1_2_8_5_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00486a006"
    },
    {
      "key": "e_1_2_8_6_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1432-1033.1993.tb18382.x"
    },
    {
      "key": "e_1_2_8_7_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi970185v"
    },
    {
      "key": "e_1_2_8_8_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/j.1460-2075.1992.tb05579.x"
    },
    {
      "key": "e_1_2_8_9_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/j.1460-2075.1996.tb00350.x"
    },
    {
      "key": "e_1_2_8_10_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1023/A:1026317612554"
    },
    {
      "key": "e_1_2_8_11_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0167-4889(98)00152-9"
    },
    {
      "key": "e_1_2_8_12_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0021-9258(18)62016-2"
    },
    {
      "key": "e_1_2_8_13_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2364(82)90279-7"
    },
    {
      "key": "e_1_2_8_14_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0006-291X(83)91225-1"
    },
    {
      "key": "e_1_2_8_15_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/ja00231a044"
    },
    {
      "key": "e_1_2_8_16_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2364(85)90018-6"
    },
    {
      "key": "e_1_2_8_17_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2364(81)90037-8"
    },
    {
      "key": "e_1_2_8_18_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1023/A:1018315729609"
    },
    {
      "key": "e_1_2_8_19_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0014-5793(87)80948-1"
    },
    {
      "key": "e_1_2_8_20_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2364(89)90341-7"
    },
    {
      "key": "e_1_2_8_21_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1002/bip.360291009"
    },
    {
      "key": "e_1_2_8_22_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/0022-2836(91)90214-Q"
    },
    {
      "key": "e_1_2_8_23_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1016/S0076-6879(94)39014-2"
    },
    {
      "key": "e_1_2_8_24_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1146/annurev.bi.47.070178.001343"
    },
    {
      "key": "e_1_2_8_25_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/nsb0694-399"
    },
    {
      "key": "e_1_2_8_26_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jmbi.1994.0023"
    },
    {
      "key": "e_1_2_8_27_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jmbi.1994.0024"
    },
    {
      "key": "e_1_2_8_28_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/bbrc.1996.0693"
    },
    {
      "key": "e_1_2_8_29_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00152a015"
    },
    {
      "key": "e_1_2_8_30_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1051/epn/19861701011"
    },
    {
      "key": "e_1_2_8_31_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/BF00227466"
    },
    {
      "key": "e_1_2_8_32_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1007/BF00227471"
    },
    {
      "key": "e_1_2_8_33_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1021/bi00069a025"
    },
    {
      "key": "e_1_2_8_34_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.3381086"
    },
    {
      "key": "e_1_2_8_35_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1399-3011.1993.tb00470.x"
    },
    {
      "key": "e_1_2_8_36_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1126/science.8178170"
    },
    {
      "key": "e_1_2_8_37_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1006/jmbi.1997.1322"
    },
    {
      "key": "e_1_2_8_38_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1111/j.1399-3011.1995.tb01322.x"
    },
    {
      "key": "e_1_2_8_39_2",
      "doi-asserted-by": "publisher",
      "DOI": "10.1038/nsb0397-180"
    }
  ],
  "container-title": "European Journal of Biochemistry",
  "original-title": [],
  "language": "en",
  "link": [
    {
      "URL": "https://api.wiley.com/onlinelibrary/tdm/v1/articles/10.1046%2Fj.1432-1327.2000.01380.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "text-mining"
    },
    {
      "URL": "https://febs.onlinelibrary.wiley.com/doi/pdf/10.1046/j.1432-1327.2000.01380.x",
      "content-type": "unspecified",
      "content-version": "vor",
      "intended-application": "similarity-checking"
    }
  ],
  "deposited": {
    "date-parts": [
      [
        2023,
        10,
        16
      ]
    ],
    "date-time": "2023-10-16T01:17:51Z",
    "timestamp": 1697419071000
  },
  "score": 1,
  "resource": {
    "primary": {
      "URL": "https://febs.onlinelibrary.wiley.com/doi/10.1046/j.1432-1327.2000.01380.x"
    }
  },
  "subtitle": [
    "An NMR\u2010analysis of thymosin \u03b24 mutants in solution and correlation with their biological activity"
  ],
  "short-title": [],
  "issued": {
    "date-parts": [
      [
        2000,
        6
      ]
    ]
  },
  "references-count": 38,
  "journal-issue": {
    "issue": "12",
    "published-print": {
      "date-parts": [
        [
          2000,
          6
        ]
      ]
    }
  },
  "alternative-id": [
    "10.1046/j.1432-1327.2000.01380.x"
  ],
  "URL": "http://dx.doi.org/10.1046/j.1432-1327.2000.01380.x",
  "relation": {},
  "ISSN": [
    "0014-2956",
    "1432-1033"
  ],
  "subject": [],
  "container-title-short": "European Journal of Biochemistry",
  "published": {
    "date-parts": [
      [
        2000,
        6
      ]
    ]
  }
}