NMR assignment of intrinsically disordered self-processing
module of the FrpC protein of Neisseria meningitidis

J 2015

NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis

KUBÁŇ, Vojtěch, Jiří NOVÁČEK, Ladislav BUMBA and Lukáš ŽÍDEK

Basic information

Original name

NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis

Authors

KUBÁŇ, Vojtěch (203 Czech Republic, guarantor, belonging to the institution), Jiří NOVÁČEK (203 Czech Republic, belonging to the institution), Ladislav BUMBA (203 Czech Republic) and Lukáš ŽÍDEK (203 Czech Republic, belonging to the institution)

Edition

Biomolecular NMR Assignments, Dordrecht (Netherlands), Springer Netherlands, 2015, 1874-2718

Other information

Language

English

Type of outcome

Článek v odborném periodiku

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

není předmětem státního či obchodního tajemství

References:

URL

Impact factor

Impact factor: 0.687

RIV identification code

RIV/00216224:14740/15:00085528

Organization unit

Central European Institute of Technology

DOI

http://dx.doi.org/10.1007/s12104-015-9625-z

UT WoS

000361440100046

Keywords in English

FrpC; Self-processing module; Neisseria meningitidis; Intrinsically disordered proteins; Sparse sampling; Resolution-enhanced spectroscopy; Resonance assignment

Abstract

V originále

The self-processing module (SPM) is an internal segment of the FrpC protein (P415-F591) secreted by the pathogenic Gram-negative bacterium Neisseria meningitidis during meningococcal infection of human upper respiratory tract. SPM mediates 'protein trans-splicing', a unique natural mechanism for editing of proteins, which involves a calcium-dependent autocatalytic cleavage of the peptide bond between D414 and P415 and covalent linkage of the cleaved fragment through its carboxy-terminal group of D414 to -amino group of lysine residue within a neighboring polypeptide chain. We present an NMR resonance assignment of the calcium-free SPM, which displays characteristic features of intrinsically disordered proteins. Non-uniformly sampled 5D HN(CA)CONH, 4D HCBCACON, and HCBCANCO spectra were recorded to resolve poorly dispersed resonance frequencies of the disordered protein and 91 % of SPM residues were unambiguously assigned. Analysis of the chemical shifts revealed that two regions of the intrinsically disordered SPM (A95-S101 and R120-I127) have a tendency to form a helical structure, whereas the residues P1-D7 and G36-A40 have the propensity to adopt a beta-structure.

Links

ED1.1.00/02.0068, research and development project

Name: CEITEC - central european institute of technology

Citovat

KUBÁŇ, Vojtěch, Jiří NOVÁČEK, Ladislav BUMBA and Lukáš ŽÍDEK. NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis. Biomolecular NMR Assignments. Dordrecht (Netherlands): Springer Netherlands, 2015, vol. 9, No 2, p. 435-440. ISSN 1874-2718. Available from: https://dx.doi.org/10.1007/s12104-015-9625-z.

@article{1322749,
   author = {Kubáň, Vojtěch and Nováček, Jiří and Bumba, Ladislav and Žídek, Lukáš},
   article_location = {Dordrecht (Netherlands)},
   article_number = {2},
   doi = {http://dx.doi.org/10.1007/s12104-015-9625-z},
   keywords = {FrpC; Self-processing module; Neisseria meningitidis; Intrinsically disordered proteins; Sparse sampling; Resolution-enhanced spectroscopy; Resonance assignment},
   language = {eng},
   issn = {1874-2718},
   journal = {Biomolecular NMR Assignments},
   title = {NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis},
   url = {http://download.springer.com/static/pdf/605/art%253A10.1007%252Fs12104-015-9625-z.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs12104-015-9625-z&token2=exp=1451977460~acl=%2Fstatic%2Fpdf%2F605%2Fart%25253A10.1007%25252Fs12104-015-96},
   volume = {9},
   year = {2015}
}

TY  - JOUR
ID  - 1322749
AU  - Kubáň, Vojtěch - Nováček, Jiří - Bumba, Ladislav - Žídek, Lukáš
PY  - 2015
TI  - NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis
JF  - Biomolecular NMR Assignments
VL  - 9
IS  - 2
SP  - 435-440
EP  - 435-440
PB  - Springer Netherlands
SN  - 18742718
KW  - FrpC
KW  - Self-processing module
KW  - Neisseria meningitidis
KW  - Intrinsically disordered proteins
KW  - Sparse sampling
KW  - Resolution-enhanced spectroscopy
KW  - Resonance assignment
UR  - http://download.springer.com/static/pdf/605/art%253A10.1007%252Fs12104-015-9625-z.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs12104-015-9625-z&token2=exp=1451977460~acl=%2Fstatic%2Fpdf%2F605%2Fart%25253A10.1007%25252Fs12104-015-96
L2  - http://download.springer.com/static/pdf/605/art%253A10.1007%252Fs12104-015-9625-z.pdf?originUrl=http%3A%2F%2Flink.springer.com%2Farticle%2F10.1007%2Fs12104-015-9625-z&token2=exp=1451977460~acl=%2Fstatic%2Fpdf%2F605%2Fart%25253A10.1007%25252Fs12104-015-96
N2  - The self-processing module (SPM) is an internal segment of the FrpC protein (P415-F591) secreted by the pathogenic Gram-negative bacterium Neisseria meningitidis during meningococcal infection of human upper respiratory tract. SPM mediates 'protein trans-splicing', a unique natural mechanism for editing of proteins, which involves a calcium-dependent autocatalytic cleavage of the peptide bond between D414 and P415 and covalent linkage of the cleaved fragment through its carboxy-terminal group of D414 to -amino group of lysine residue within a neighboring polypeptide chain. We present an NMR resonance assignment of the calcium-free SPM, which displays characteristic features of intrinsically disordered proteins. Non-uniformly sampled 5D HN(CA)CONH, 4D HCBCACON, and HCBCANCO spectra were recorded to resolve poorly dispersed resonance frequencies of the disordered protein and 91 % of SPM residues were unambiguously assigned. Analysis of the chemical shifts revealed that two regions of the intrinsically disordered SPM (A95-S101 and R120-I127) have a tendency to form a helical structure, whereas the residues P1-D7 and G36-A40 have the propensity to adopt a beta-structure.
ER  -

KUBÁŇ, Vojtěch, Jiří NOVÁČEK, Ladislav BUMBA and Lukáš ŽÍDEK. NMR assignment of intrinsically disordered self-processing module of the FrpC protein of Neisseria meningitidis. \textit{Biomolecular NMR Assignments}. Dordrecht (Netherlands): Springer Netherlands, 2015, vol.~9, No~2, p.~435-440. ISSN~1874-2718. Available from: https://dx.doi.org/10.1007/s12104-015-9625-z.

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