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

Article in a journal

Field of Study

10600 1.6 Biological sciences

Country of publisher

Netherlands

Confidentiality degree

is not subject to a state or trade secret

References:

URL

Impact factor

Impact factor: 0.687

RIV identification code

RIV/00216224:14740/15:00085528

Organization unit

Central European Institute of Technology

DOI

https://doi.org/10.1007/s12104-015-9625-z

UT WoS

000361440100046

EID Scopus

2-s2.0-84941998089

Keywords in English

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

Abstract

In the original language

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

Cite

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://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 = {https://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://doi.org/10.1007/s12104-015-9625-z.

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