Go to:
Logótipo
Você está em: Start > Publications > View > THE 12.3 KDA SUBUNIT OF COMPLEX-I (RESPIRATORY-CHAIN NADH DEHYDROGENASE) FROM NEUROSPORA-CRASSA - CDNA CLONING AND CHROMOSOMAL MAPPING OF THE GENE
Map of Premises
Principal
Publication

THE 12.3 KDA SUBUNIT OF COMPLEX-I (RESPIRATORY-CHAIN NADH DEHYDROGENASE) FROM NEUROSPORA-CRASSA - CDNA CLONING AND CHROMOSOMAL MAPPING OF THE GENE

Title
THE 12.3 KDA SUBUNIT OF COMPLEX-I (RESPIRATORY-CHAIN NADH DEHYDROGENASE) FROM NEUROSPORA-CRASSA - CDNA CLONING AND CHROMOSOMAL MAPPING OF THE GENE
Type
Article in International Scientific Journal
Year
1993
Authors
azevedo, je
(Author)
ICBAS
View Personal Page You do not have permissions to view the institutional email. Search for Participant Publications View Authenticus page Without ORCID
werner, s
(Author)
Other
The person does not belong to the institution. The person does not belong to the institution. The person does not belong to the institution. Without AUTHENTICUS Without ORCID
cabral, p
(Author)
Other
The person does not belong to the institution. The person does not belong to the institution. The person does not belong to the institution. Without AUTHENTICUS Without ORCID
Journal
Title: Biochemical JournalImported from Authenticus Search for Journal Publications
Vol. 291
Pages: 729-732
ISSN: 0264-6021
Publisher: PORTLAND PRESS LTD
Other information
Authenticus ID: P-001-N2S
Abstract (EN): The 12.3 kDa subunit of complex I (respiratory-chain NADH dehydrogenase) is a nuclear-coded protein of the hydrophobic fragment of the enzyme. We have isolated and sequenced a full-length cDNA clone coding for this polypeptide. The deduced protein is 104 amino acid residues long with a molecular mass of 12 305 Da. This particular subunit of complex I lacks a cleavable mitochondrial targeting sequence. In agreement with its localization within complex I, we have found that this subunit behaves like an intrinsic membrane protein. Nevertheless, the deduced protein is rather hydrophilic, exhibiting no hydrophobic domain long enough to traverse a membrane in an alpha-helical conformation. The 12.3 kDa subunit shows a significant similarity to the hinge protein of complex III, suggesting that these two polypeptides may be involved in identical functions. This complex I subunit is coded for by a single gene. Applying restriction-fragment-length-polymorphism mapping, we located the gene on the right side of the centromere in linkage group I, linked to the lys-4 locus.
Language: English
Type (Professor's evaluation): Scientific
No. of pages: 4
Documents
We could not find any documents associated to the publication.
Related Publications

Of the same journal

Two new FUT2 (fucosyltransferase 2 gene) missense polymorphisms, 739G -> A and 839T -> C, are partly responsible for non-secretor status in a Caucasian population from Northern Portugal (2004)
Article in International Scientific Journal
Serpa, J; Mendes, N; Celso Reis; Santos-Silva F; Raquel Almeida; Le Pendu, J; David L
The 12.3-kDa subunit of complex I from Neurospora crassa: cDNA cloning and chromossomal mapping of the gene. (1993)
Article in International Scientific Journal
Arnaldo Videira; J E Azevedo; Sigurd Werner; Ana Cabral
The Leishmania infantum cytosolic SIR2-related protein 1 (LiSIR2RP1) is an NAD(+)-dependent deacetylase and ADP-ribosyltransferase (2008)
Article in International Scientific Journal
Joana Tavares; Ali Ouaissi; Nuno Santarem; Denis Sereno; Baptiste Vergnes; Paula Sampaio; Anabela Cordeiro Da Silva
The internal alternative NADH dehydrogenase of Neurospora crassa mitochondria (2003)
Article in International Scientific Journal
duarte, m; peters, m; schulte, u; videira, a
The glycation site specificity of human serum transferrin is a determinant for transferrin's functional impairment under elevated glycaemic conditions (2014)
Article in International Scientific Journal
Andre M N Silva; Paulo R H Sousa; Joao T S Coimbra; Natercia F Bras; Rui Vitorino; Pedro A Fernandes; Maria J Ramos; Maria Rangel; Pedro Domingues

See all (21)

Recommend this page Top
Copyright 1996-2025 © Faculdade de Medicina Dentária da Universidade do Porto  I Terms and Conditions  I Acessibility  I Index A-Z  I Guest Book
Page created on: 2025-07-01 at 18:40:39 | Acceptable Use Policy | Data Protection Policy | Complaint Portal